Found 717 chains in Knotoided chains table. Displaying 1 - 150. Applied filters: Probabilistic

Search results query: topological notation for knotoids: K 3.1, 2.1

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#pdbid|chain|deposition date|is S/K-not|(slip)knot types;
      
  6eea|A|2018-12-02|K|3.1 2.1;
  6ebe|A|2018-12-02|K|3.1 2.1;
  6eda|A|2018-12-02|K|3.1 2.1;
  6eeo|A|2018-12-02|K|3.1 2.1;
  6eeh|A|2018-12-02|K|3.1 2.1;
  6ecz|A|2018-12-02|K|3.1 2.1;
  6g3q|A|2018-12-02|K|3.1 2.1;
  5thi|A|2018-10-25|K|3.1 2.1;
  4knj|A|2018-10-21|K|3.1 2.1;
  4qiz|A|2018-10-21|K|3.1 2.1;
  1bn1|A|2018-10-21|K|3.1 2.1;
  5n25|A|2018-10-21|K|3.1 2.1;
  5ohh|A|2018-10-21|K|3.1 2.1;
  1cak|A|2018-10-21|K|3.1 2.1;
  1rzb|A|2018-10-21|K|3.1 2.1;
  4qsj|A|2018-10-21|K|3.1 2.1;
  1bv3|A|2018-10-21|K|3.1 2.1;
  1ttm|A|2018-10-21|K|3.1 2.1;
  5nea|A|2018-10-21|K|3.1 2.1;
  5fl5|A|2018-10-21|K|3.1 2.1;
  1bnn|A|2018-10-21|K|3.1 2.1;
  4ygl|A|2018-10-21|K|3.1 2.1;
  3iqk|A|2018-10-21|K|3.1 2.1;
  6b59|A|2018-10-21|K|3.1 2.1;
  3mnk|A|2018-10-20|K|3.1 2.1;
  1g3z|A|2018-10-20|K|3.1 2.1;
  2nnv|A|2018-10-20|K|3.1 2.1;
  3dc9|A|2018-10-20|K|3.1 2.1;
  3daz|A|2018-10-20|K|3.1 2.1;
  2cba|A|2018-10-20|K|3.1 2.1;
  3s72|B|2018-10-20|K|3.1 2.1;
  2cbd|A|2018-10-20|K|3.1 2.1;
  3nj9|A|2018-10-20|K|3.1 2.1;
  4e3h|A|2018-10-20|K|3.1 2.1;
  4ca2|A|2018-10-20|K|3.1 2.1;
  4fpt|A|2018-10-20|K|3.1 2.1;
  3r17|B|2018-10-20|K|3.1 2.1;
  4zwz|A|2018-10-20|K|3.1 2.1;
  4q07|A|2018-10-20|K|3.1 2.1;
  5g01|A|2018-10-20|K|3.1 2.1;
  4mdl|A|2018-10-20|K|3.1 2.1;
  5tt3|A|2018-10-20|K|3.1 2.1;
  5umc|A|2018-10-20|K|3.1 2.1;
  4q09|A|2018-10-20|K|3.1 2.1;
  1g46|A|2018-10-20|K|3.1 2.1;
  5ogp|A|2018-10-20|K|3.1 2.1;
  1if6|A|2018-10-20|K|3.1 2.1;
  6eki|A|2018-10-20|K|3.1 2.1;
  3igp|A|2018-10-20|K|3.1 2.1;
  5fnh|A|2018-10-20|K|3.1 2.1;
  3w6h|A|2018-10-20|K|3.1 2.1;
  5clu|A|2018-10-20|K|3.1 2.1;
  1i9n|A|2018-10-20|K|3.1 2.1;
  3mhc|A|2018-10-20|K|3.1 2.1;
  5fls|A|2018-10-20|K|3.1 2.1;
  1cnj|A|2018-10-20|K|3.1 2.1;
  1if4|A|2018-10-20|K|3.1 2.1;
  4k0t|A|2018-10-20|K|3.1 2.1;
  4qsb|A|2018-10-20|K|3.1 2.1;
  4k0s|A|2018-10-20|K|3.1 2.1;
  3mna|A|2018-10-20|K|3.1 2.1;
  4n0x|B|2018-10-20|K|3.1 2.1;
  3mzc|A|2018-10-20|K|3.1 2.1;
  5msa|A|2018-10-20|K|3.1 2.1;
  5nee|A|2018-10-20|K|3.1 2.1;
  2hfw|A|2018-10-20|K|3.1 2.1;
  2f14|A|2018-10-20|K|3.1 2.1;
  3d92|A|2018-10-20|K|3.1 2.1;
  4m2r|A|2018-10-20|K|3.1 2.1;
  5ljq|A|2018-10-20|K|3.1 2.1;
  3kon|A|2018-10-20|K|3.1 2.1;
  4qk2|A|2018-10-20|K|3.1 2.1;
  4z0q|A|2018-10-20|K|3.1 2.1;
  6fe2|A|2018-10-20|K|3.1 2.1;
  4gl1|X|2018-10-20|K|3.1 2.1;
  2nwo|A|2018-10-20|K|3.1 2.1;
  1th9|A|2018-10-20|K|3.1 2.1;
  1cao|A|2018-10-20|K|3.1 2.1;
  4bf1|A|2018-10-20|K|3.1 2.1;
  3dc3|A|2018-10-20|K|3.1 2.1;
  2nno|A|2018-10-20|K|3.1 2.1;
  4qj0|A|2018-10-20|K|3.1 2.1;
  4cnv|A|2018-10-20|K|3.1 2.1;
  4r59|A|2018-10-20|K|3.1 2.1;
  4mlt|A|2018-10-20|K|3.1 2.1;
  3mnu|A|2018-10-20|K|3.1 2.1;
  3s75|B|2018-10-20|K|3.1 2.1;
  4mdg|A|2018-10-20|K|3.1 2.1;
  5eij|A|2018-10-20|K|3.1 2.1;
  3v2j|A|2018-10-20|K|3.1 2.1;
  3ml5|A|2018-10-20|K|3.1 2.1;
  1cni|A|2018-10-20|K|3.1 2.1;
  2hoc|A|2018-10-20|K|3.1 2.1;
  4yxi|A|2018-10-20|K|3.1 2.1;
  5fnl|A|2018-10-20|K|3.1 2.1;
  4xz5|A|2018-10-20|K|3.1 2.1;
  4q7p|A|2018-10-20|K|3.1 2.1;
  5flr|A|2018-10-20|K|3.1 2.1;
  5flp|A|2018-10-20|K|3.1 2.1;
  4k0z|A|2018-10-20|K|3.1 2.1;
  5e2s|A|2018-10-20|K|3.1 2.1;
  2gd8|A|2018-10-20|K|3.1 2.1;
  6equ|A|2018-10-20|K|3.1 2.1;
  5jgs|B|2018-10-20|K|3.1 2.1;
  5fnj|A|2018-10-20|K|3.1 2.1;
  1lgd|A|2018-10-20|K|3.1 2.1;
  4ygn|A|2018-10-20|K|3.1 2.1;
  4z1n|A|2018-10-20|K|3.1 2.1;
  3fe4|A|2018-10-20|K|3.1 2.1;
  5lmd|A|2018-10-20|K|3.1 2.1;
  1ze8|A|2018-10-20|K|3.1 2.1;
  4k13|A|2018-10-20|K|3.1 2.1;
  3ryj|B|2018-10-20|K|3.1 2.1;
  1te3|X|2018-10-20|K|3.1 2.1;
  3rz1|B|2018-10-20|K|3.1 2.1;
  5sz5|A|2018-10-20|K|3.1 2.1;
  1fql|A|2018-10-20|K|3.1 2.1;
  1z97|A|2018-10-20|K|3.1 2.1;
  5cjf|A|2018-10-20|K|3.1 2.1;
  5txy|A|2018-10-20|K|3.1 2.1;
  1fsq|A|2018-10-20|K|3.1 2.1;
  4q49|A|2018-10-20|K|3.1 2.1;
  1bn4|A|2018-10-20|K|3.1 2.1;
  5bu6|B|2018-10-20|K|3.1 2.1;
  3ryv|B|2018-10-20|K|3.1 2.1;
  2foq|A|2018-10-20|K|3.1 2.1;
  5th4|A|2018-10-20|K|3.1 2.1;
  1yo0|A|2018-10-20|K|3.1 2.1;
  5flo|A|2018-10-20|K|3.1 2.1;
  4qk1|A|2018-10-20|K|3.1 2.1;
  3gz0|A|2018-10-20|K|3.1 2.1;
  5jes|B|2018-10-20|K|3.1 2.1;
  6b5a|A|2018-10-20|K|3.1 2.1;
  2nng|A|2018-10-20|K|3.1 2.1;
  3p3j|A|2018-10-20|K|3.1 2.1;
  5fdi|A|2018-10-20|K|3.1 2.1;
  3mni|A|2018-10-20|K|3.1 2.1;
  1ugd|A|2018-10-20|K|3.1 2.1;
  2x7s|A|2018-10-20|K|3.1 2.1;
  2fnn|A|2018-10-20|K|3.1 2.1;
  5jdf|A|2018-10-20|K|3.1 2.1;
  3mnj|A|2018-10-20|K|3.1 2.1;
  3hlj|A|2018-10-20|K|3.1 2.1;
  3oik|A|2018-10-20|K|3.1 2.1;
  3hkn|A|2018-10-20|K|3.1 2.1;
  3u3a|X|2018-10-20|K|3.1 2.1;
  4qk3|A|2018-10-20|K|3.1 2.1;
  4kp5|A|2018-10-20|K|3.1 2.1;
  5jep|B|2018-10-20|K|3.1 2.1;
  4rn4|A|2018-10-20|K|3.1 2.1;
  4z1e|A|2018-10-20|K|3.1 2.1;
  5eh5|A|2018-10-20|K|3.1 2.1;
  4xe1|A|2018-10-20|K|3.1 2.1;
  5ekh|A|2018-10-20|K|3.1 2.1;
  1bn3|A|2018-10-20|K|3.1 2.1;
  1zsc|A|2018-10-20|K|3.1 2.1;
  2vvb|X|2018-10-20|K|3.1 2.1;
  1cah|A|2018-10-19|K|3.1 2.1;
  5wlr|A|2018-10-19|K|3.1 2.1;
  1fr4|A|2018-10-19|K|3.1 2.1;
  4q90|A|2018-10-19|K|3.1 2.1;
  5amg|A|2018-10-19|K|3.1 2.1;
  4fvn|A|2018-10-19|K|3.1 2.1;
  3vbd|A|2018-10-19|K|3.1 2.1;
  4q7w|A|2018-10-19|K|3.1 2.1;
  3k7k|A|2018-10-19|K|3.1 2.1;
  3v3i|B|2018-10-19|K|3.1 2.1;
  3r16|A|2018-10-19|K|3.1 2.1;
  6g4t|A|2018-10-19|K|3.1 2.1;
  1xq0|A|2018-10-19|K|3.1 2.1;
  5a25|A|2018-10-19|K|3.1 2.1;
  4jsa|A|2018-10-19|K|3.1 2.1;
  2fnm|A|2018-10-19|K|3.1 2.1;
  4rh2|A|2018-10-19|K|3.1 2.1;
  1raz|A|2018-10-19|K|3.1 2.1;
  4q78|A|2018-10-19|K|3.1 2.1;
  4yxu|A|2018-10-19|K|3.1 2.1;
  1caz|A|2018-10-19|K|3.1 2.1;
  3qyk|A|2018-10-19|K|3.1 2.1;
  3ryx|B|2018-10-19|K|3.1 2.1;
  4q8y|A|2018-10-19|K|3.1 2.1;
  5e2r|A|2018-10-19|K|3.1 2.1;
  1t9n|A|2018-10-19|K|3.1 2.1;
  6fe1|A|2018-10-19|K|3.1 2.1;
  5ca2|A|2018-10-19|K|3.1 2.1;
  5flq|A|2018-10-19|K|3.1 2.1;
  2fmz|A|2018-10-19|K|3.1 2.1;
  4pyx|A|2018-10-19|K|3.1 2.1;
  2hnc|A|2018-10-19|K|3.1 2.1;
  5jq0|A|2018-10-19|K|3.1 2.1;
  5n1r|A|2018-10-19|K|3.1 2.1;
  5bnl|A|2018-10-19|K|3.1 2.1;
  3hku|A|2018-10-19|K|3.1 2.1;
  4kuy|A|2018-10-19|K|3.1 2.1;
  4ilx|A|2018-10-19|K|3.1 2.1;
  4zx1|A|2018-10-19|K|3.1 2.1;
  3dvd|A|2018-10-19|K|3.1 2.1;
  1h9n|A|2018-10-19|K|3.1 2.1;
  1g0f|A|2018-10-19|K|3.1 2.1;
  3v2m|A|2018-10-19|K|3.1 2.1;
  3v3h|B|2018-10-19|K|3.1 2.1;
  1v9i|C|2018-10-19|K|3.1 2.1;
  5uln|A|2018-10-19|K|3.1 2.1;
  4qy3|A|2018-10-19|K|3.1 2.1;
  5u0f|A|2018-10-19|K|3.1 2.1;
  2wd3|A|2018-10-19|K|3.1 2.1;
  5vgy|A|2018-10-19|K|3.1 2.1;
  5fdc|A|2018-10-19|K|3.1 2.1;
  3s78|B|2018-10-19|K|3.1 2.1;
  4mo8|A|2018-10-19|K|3.1 2.1;
  4e5q|A|2018-10-19|K|3.1 2.1;
  4g0c|A|2018-10-19|K|3.1 2.1;
  5u0d|A|2018-10-19|K|3.1 2.1;
  3n0n|A|2018-10-19|K|3.1 2.1;
  4mdm|A|2018-10-19|K|3.1 2.1;
  5dsi|A|2018-10-19|K|3.1 2.1;
  5jgt|B|2018-10-19|K|3.1 2.1;
  5a6h|A|2018-10-19|K|3.1 2.1;
  3m1j|A|2018-10-19|K|3.1 2.1;
  4idr|X|2018-10-19|K|3.1 2.1;
  3dd0|A|2018-10-19|K|3.1 2.1;
  1okm|A|2018-10-19|K|3.1 2.1;
  5llc|A|2018-10-19|K|3.1 2.1;
  4q8z|A|2018-10-19|K|3.1 2.1;
  3mmf|A|2018-10-19|K|3.1 2.1;
  5jn1|A|2018-10-19|K|3.1 2.1;
  4qjm|A|2018-10-19|K|3.1 2.1;
  4rux|A|2018-10-19|K|3.1 2.1;
  6cjv|A|2018-10-19|K|3.1 2.1;
  3hs4|A|2018-10-19|K|3.1 2.1;
  3sbh|A|2018-10-19|K|3.1 2.1;
  5jg5|B|2018-10-19|K|3.1 2.1;
  4mlx|A|2018-10-19|K|3.1 2.1;
  3s71|B|2018-10-19|K|3.1 2.1;
  4kni|A|2018-10-19|K|3.1 2.1;
  2q1b|A|2018-10-19|K|3.1 2.1;
  3dv7|A|2018-10-19|K|3.1 2.1;
  4cnr|A|2018-10-19|K|3.1 2.1;
  3ks3|A|2018-10-19|K|3.1 2.1;
  6bbs|A|2018-10-19|K|3.1 2.1;
  3v7x|A|2018-10-19|K|3.1 2.1;
  4ht2|A|2018-10-19|K|3.1 2.1;
  1cal|A|2018-10-19|K|3.1 2.1;
  4qtl|A|2018-10-19|K|3.1 2.1;
  4qsi|A|2018-10-19|K|3.1 2.1;
  3p5l|A|2018-10-19|K|3.1 2.1;
  3s74|B|2018-10-19|K|3.1 2.1;
  3hkq|A|2018-10-19|K|3.1 2.1;
  2fnk|A|2018-10-19|K|3.1 2.1;
  4iwz|A|2018-10-19|K|3.1 2.1;
  5ti0|A|2018-10-19|K|3.1 2.1;
  5dsj|A|2018-10-19|K|3.1 2.1;
  3sap|A|2018-10-19|K|3.1 2.1;
  4q7v|A|2018-10-19|K|3.1 2.1;
  3s9t|A|2018-10-19|K|3.1 2.1;
  4r5a|A|2018-10-19|K|3.1 2.1;
  4qjw|A|2018-10-19|K|3.1 2.1;
  5fnm|A|2018-10-19|K|3.1 2.1;
  5jn7|A|2018-10-19|K|3.1 2.1;
  4m2u|A|2018-10-19|K|3.1 2.1;
  3n2p|A|2018-10-19|K|3.1 2.1;
  5ll9|A|2018-10-19|K|3.1 2.1;
  1g48|A|2018-10-19|K|3.1 2.1;
  3m5t|A|2018-10-19|K|3.1 2.1;
  1cai|A|2018-10-19|K|3.1 2.1;
  1ray|A|2018-10-19|K|3.1 2.1;
  5fni|A|2018-10-19|K|3.1 2.1;
  4yx4|A|2018-10-19|K|3.1 2.1;
  3t5z|A|2018-10-19|K|3.1 2.1;
  4zao|A|2018-10-19|K|3.1 2.1;
  6b00|A|2018-10-19|K|3.1 2.1;
  5g0b|A|2018-10-19|K|3.1 2.1;
  1eou|A|2018-10-19|K|3.1 2.1;
  3oyq|A|2018-10-19|K|3.1 2.1;
  4lhi|A|2018-10-19|K|3.1 2.1;
  5fl6|A|2018-10-19|K|3.1 2.1;
  2pou|A|2018-10-19|K|3.1 2.1;
  5e2n|A|2018-10-19|K|3.1 2.1;
  5eh8|A|2018-10-19|K|3.1 2.1;
  1am6|A|2018-10-19|K|3.1 2.1;
  5aml|A|2018-10-19|K|3.1 2.1;
  1g53|A|2018-10-19|K|3.1 2.1;
  4js6|A|2018-10-19|K|3.1 2.1;
  4jss|A|2018-10-19|K|3.1 2.1;
  1bnt|A|2018-10-19|K|3.1 2.1;
  1bzm|A|2018-10-19|K|3.1 2.1;
  4kp8|A|2018-10-19|K|3.1 2.1;
  4hey|A|2018-10-19|K|3.1 2.1;
  2vva|X|2018-10-19|K|3.1 2.1;
  5ehv|A|2018-10-19|K|3.1 2.1;
  1mua|A|2018-10-19|K|3.1 2.1;
  4z1k|A|2018-10-19|K|3.1 2.1;
  1g45|A|2018-10-19|K|3.1 2.1;
  4q81|A|2018-10-19|K|3.1 2.1;
  4dz7|A|2018-10-19|K|3.1 2.1;
  4e3f|A|2018-10-19|K|3.1 2.1;
  4jsz|A|2018-10-19|K|3.1 2.1;
  2eu2|A|2018-10-19|K|3.1 2.1;
  5tuo|A|2018-10-19|K|3.1 2.1;
  4n16|A|2018-10-19|K|3.1 2.1;
  5e2k|A|2018-10-19|K|3.1 2.1;
  2nns|A|2018-10-19|K|3.1 2.1;
  5jeh|B|2018-10-19|K|3.1 2.1;
  3m1q|A|2018-10-19|K|3.1 2.1;
  3myq|A|2018-10-19|K|3.1 2.1;
  1zsb|A|2018-10-19|K|3.1 2.1;
  1okn|A|2018-10-19|K|3.1 2.1;
  6d1l|A|2018-10-19|K|3.1 2.1;
  5jmz|A|2018-10-19|K|3.1 2.1;
  4hu1|A|2018-10-19|K|3.1 2.1;
  4knn|A|2018-10-18|K|3.1 2.1;
  5e28|A|2018-10-18|K|3.1 2.1;
  5ll5|A|2018-10-18|K|3.1 2.1;
  5lla|A|2018-10-18|K|3.1 2.1;
  5zxw|A|2018-10-18|K|3.1 2.1;
  5jqt|A|2018-10-18|K|3.1 2.1;
  1cam|A|2018-10-18|K|3.1 2.1;
  6b4d|A|2018-10-18|K|3.1 2.1;
  1caj|A|2018-10-18|K|3.1 2.1;
  1rze|A|2018-10-18|K|3.1 2.1;
  1lzv|A|2018-10-18|K|3.1 2.1;
  1teu|X|2018-10-18|K|3.1 2.1;
  1kwr|A|2018-10-18|K|3.1 2.1;
  2pow|A|2018-10-18|K|3.1 2.1;
  1tg3|A|2018-10-18|K|3.1 2.1;
  3oy0|A|2018-10-18|K|3.1 2.1;
  3p3h|A|2018-10-18|K|3.1 2.1;
  3dvb|A|2018-10-18|K|3.1 2.1;
  3oim|A|2018-10-18|K|3.1 2.1;
  3rge|A|2018-10-18|K|3.1 2.1;
  3rg4|A|2018-10-18|K|3.1 2.1;
  3rg3|A|2018-10-18|K|3.1 2.1;
  4hez|A|2018-10-18|K|3.1 2.1;
  4cac|A|2018-10-18|K|3.1 2.1;
  4itp|A|2018-10-18|K|3.1 2.1;
  4l5w|A|2018-10-18|K|3.1 2.1;
  4q0l|A|2018-10-18|K|3.1 2.1;
  4rfd|A|2018-10-18|K|3.1 2.1;
  3oys|A|2018-10-18|K|3.1 2.1;
  4zx0|A|2018-10-18|K|3.1 2.1;
  5ekm|A|2018-10-18|K|3.1 2.1;
  5c8i|A|2018-10-18|K|3.1 2.1;
  5j8z|A|2018-10-18|K|3.1 2.1;
  5byi|A|2018-10-18|K|3.1 2.1;
  5jeg|B|2018-10-18|K|3.1 2.1;
  5je7|B|2018-10-18|K|3.1 2.1;
  5jg3|B|2018-10-18|K|3.1 2.1;
  5mjn|A|2018-10-18|K|3.1 2.1;
  5wg7|A|2018-10-18|K|3.1 2.1;
  6bc9|A|2018-10-18|K|3.1 2.1;
  2hl4|A|2018-10-18|K|3.1 2.1;
  3p5a|A|2018-10-18|K|3.1 2.1;
  3p58|A|2018-10-18|K|3.1 2.1;
  3mnh|A|2018-10-18|K|3.1 2.1;
  2aw1|A|2018-10-18|K|3.1 2.1;
  2hkk|A|2018-10-18|K|3.1 2.1;
  1i9l|A|2018-10-18|K|3.1 2.1;
  1i9q|A|2018-10-18|K|3.1 2.1;
  3dcc|A|2018-10-18|K|3.1 2.1;
  4cq0|A|2018-10-18|K|3.1 2.1;
  3kwa|A|2018-10-18|K|3.1 2.1;
  4xiw|A|2018-10-18|K|3.1 2.1;
  4cnx|A|2018-10-18|K|3.1 2.1;
  4zwx|A|2018-10-18|K|3.1 2.1;
  4xfw|A|2018-10-18|K|3.1 2.1;
  5ogo|A|2018-10-18|K|3.1 2.1;
  5wex|A|2018-10-18|K|3.1 2.1;
  2weo|A|2018-10-18|K|3.1 2.1;
  5fng|A|2018-10-18|K|3.1 2.1;
  1bnv|A|2018-10-18|K|3.1 2.1;
  3uyq|A|2018-10-18|K|3.1 2.1;
  5fnk|A|2018-10-18|K|3.1 2.1;
  5brw|A|2018-10-18|K|3.1 2.1;
  5llh|A|2018-10-18|K|3.1 2.1;
  1z93|A|2018-10-18|K|3.1 2.1;
  4hew|A|2018-10-18|K|3.1 2.1;
  5n0e|A|2018-10-18|K|3.1 2.1;
  4qef|A|2018-10-18|K|3.1 2.1;
  5amd|A|2018-10-18|K|3.1 2.1;
  3oku|A|2018-10-18|K|3.1 2.1;
  3tvn|X|2018-10-18|K|3.1 2.1;
  5yui|A|2018-10-18|K|3.1 2.1;
  6g98|A|2018-10-18|K|3.1 2.1;
  5dvx|A|2018-10-18|K|3.1 2.1;
  5g0c|A|2018-10-18|K|3.1 2.1;
  5ty8|A|2018-10-18|K|3.1 2.1;
  3s77|B|2018-10-18|K|3.1 2.1;
  5dsl|A|2018-10-18|K|3.1 2.1;
  5dsm|A|2018-10-18|K|3.1 2.1;
  2hfx|A|2018-10-18|K|3.1 2.1;
  3ml2|A|2018-10-18|K|3.1 2.1;
  2nn1|A|2018-10-18|K|3.1 2.1;
  4q8x|A|2018-10-18|K|3.1 2.1;
  3uyn|A|2018-10-18|K|3.1 2.1;
  5t71|A|2018-10-18|K|3.1 2.1;
  1lg6|A|2018-10-18|K|3.1 2.1;
  3dvc|A|2018-10-18|K|3.1 2.1;
  3oil|A|2018-10-18|K|3.1 2.1;
  1ugb|A|2018-10-18|K|3.1 2.1;
  3l14|A|2018-10-18|K|3.1 2.1;
  3p4v|A|2018-10-18|K|3.1 2.1;
  1xpz|A|2018-10-18|K|3.1 2.1;
  3hkt|A|2018-10-18|K|3.1 2.1;
  3lxe|A|2018-10-18|K|3.1 2.1;
  3p55|A|2018-10-18|K|3.1 2.1;
  3u45|X|2018-10-18|K|3.1 2.1;
  3u7c|A|2018-10-18|K|3.1 2.1;
  4zwy|A|2018-10-18|K|3.1 2.1;
  3t83|A|2018-10-18|K|3.1 2.1;
  4fik|A|2018-10-18|K|3.1 2.1;
  5ekj|A|2018-10-18|K|3.1 2.1;
  4jsw|A|2018-10-18|K|3.1 2.1;
  5eoi|A|2018-10-18|K|3.1 2.1;
  4zwi|A|2018-10-18|K|3.1 2.1;
  5fl4|A|2018-10-18|K|3.1 2.1;
  5wgp|A|2018-10-18|K|3.1 2.1;
  4q7s|A|2018-10-18|K|3.1 2.1;
  6g9u|A|2018-10-18|K|3.1 2.1;
  2ili|A|2018-10-18|K|3.1 2.1;
  3rld|A|2018-10-18|K|3.1 2.1;
  2x7t|A|2018-10-18|K|3.1 2.1;
  3k34|A|2018-10-18|K|3.1 2.1;
  2nmx|A|2018-10-18|K|3.1 2.1;
  2osm|A|2018-10-18|K|3.1 2.1;
  3rj7|A|2018-10-18|K|3.1 2.1;
  3k2f|A|2018-10-18|K|3.1 2.1;
  2wej|A|2018-10-18|K|3.1 2.1;
  4e3g|A|2018-10-18|K|3.1 2.1;
  4ruy|A|2018-10-17|K|3.1 2.1;
  3n3j|A|2018-10-17|K|3.1 2.1;
  5thn|A|2018-10-17|K|3.1 2.1;
  1bnm|A|2018-10-17|K|3.1 2.1;
  1uge|A|2018-10-17|K|3.1 2.1;
  1ccu|A|2018-10-17|K|3.1 2.1;
  2geh|A|2018-10-17|K|3.1 2.1;
  4ht0|A|2018-10-17|K|3.1 2.1;
  3s8x|A|2018-10-17|K|3.1 2.1;
  4pzh|A|2018-10-17|K|3.1 2.1;
  4qiy|A|2018-10-17|K|3.1 2.1;
  4qsa|A|2018-10-17|K|3.1 2.1;
  3sax|A|2018-10-17|K|3.1 2.1;
  4q6e|A|2018-10-17|K|3.1 2.1;
  3n4b|A|2018-10-17|K|3.1 2.1;
  4kuw|A|2018-10-17|K|3.1 2.1;
  1xeg|A|2018-10-17|K|3.1 2.1;
  4knm|A|2018-10-17|K|3.1 2.1;
  2nwp|A|2018-10-13|K|3.1 2.1;
  1h4n|A|2018-10-13|K|3.1 2.1;
  6got|A|2018-10-13|K|3.1 2.1;
  1g4j|A|2018-10-12|K|3.1 2.1;
  6faf|A|2018-10-12|K|3.1 2.1;
  3s73|B|2018-10-04|K|3.1 2.1;
  3pjj|A|2018-10-04|K|3.1 2.1;
  4e49|A|2018-10-03|K|3.1 2.1;
  5sz6|A|2018-10-03|K|3.1 2.1;
  4rfc|A|2018-10-03|K|3.1 2.1;
  4kuv|A|2018-10-03|K|3.1 2.1;
  4l5u|A|2018-10-03|K|3.1 2.1;
  4hba|A|2018-10-03|K|3.1 2.1;
  5n24|A|2018-10-03|K|3.1 2.1;
  4qjp|A|2018-10-03|K|3.1 2.1;
  3zp9|A|2018-10-03|K|3.1 2.1;
  4qjo|A|2018-10-03|K|3.1 2.1;
  5l9e|A|2018-10-03|K|3.1 2.1;
  4fvo|A|2018-10-03|K|3.1 2.1;
  4lu3|A|2018-10-03|K|3.1 2.1;
  4kv0|A|2018-10-03|K|3.1 2.1;
  4q99|A|2018-10-03|K|3.1 2.1;
  4q87|A|2018-10-03|K|3.1 2.1;
  4fu5|A|2018-10-03|K|3.1 2.1;
  4q83|A|2018-10-03|K|3.1 2.1;
  5yuj|A|2018-10-03|K|3.1 2.1;
  1kwq|A|2018-10-03|K|3.1 2.1;
  1jd0|A|2018-10-03|K|3.1 2.1;
  1g52|A|2018-10-03|K|3.1 2.1;
  1i90|A|2018-10-03|K|3.1 2.1;
  2cbb|A|2018-10-03|K|3.1 2.1;
  1i8z|A|2018-10-03|K|3.1 2.1;
  1v9e|A|2018-10-03|K|3.1 2.1;
  1g4o|A|2018-10-03|K|3.1 2.1;
  2cbc|A|2018-10-03|K|3.1 2.1;
  1i9o|A|2018-10-03|K|3.1 2.1;
  1g1d|A|2018-10-03|K|3.1 2.1;
  2fou|A|2018-10-03|K|3.1 2.1;
  1if7|A|2018-10-03|K|3.1 2.1;
  1if9|A|2018-10-03|K|3.1 2.1;
  1i91|A|2018-10-03|K|3.1 2.1;
  2ez7|A|2018-10-03|K|3.1 2.1;
  1i9m|A|2018-10-03|K|3.1 2.1;
  1g0e|A|2018-10-03|K|3.1 2.1;
  1i9p|A|2018-10-03|K|3.1 2.1;
  1if8|A|2018-10-03|K|3.1 2.1;
  2fmg|A|2018-10-03|K|3.1 2.1;
  1thk|A|2018-10-03|K|3.1 2.1;
  3eft|A|2018-10-01|K|3.1 2.1;
  3efi|A|2018-10-01|K|3.1 2.1;
  3v5g|A|2018-10-01|K|3.1 2.1;
  3dbu|A|2018-10-01|K|3.1 2.1;
  3czv|A|2018-10-01|K|3.1 2.1;
  2q1q|A|2018-10-01|K|3.1 2.1;
  4cnw|A|2018-10-01|K|3.1 2.1;
  3bl0|A|2018-10-01|K|3.1 2.1;
  2weg|A|2018-10-01|K|3.1 2.1;
  3sbi|A|2018-10-01|K|3.1 2.1;
  3d0n|A|2018-10-01|K|3.1 2.1;
  6h29|A|2018-09-30|K|3.1 2.1;
  1can|A|2018-09-29|K|3.1 2.1;
  5gmn|A|2018-09-26|K|3.1 2.1;
  2ax2|A|2018-09-26|K|3.1 2.1;
  5dsk|A|2018-09-26|K|3.1 2.1;
  5ljt|A|2018-09-26|K|3.1 2.1;
  2abe|A|2018-09-26|K|3.1 2.1;
  1f2w|A|2018-09-26|K|3.1 2.1;
  5l70|A|2018-09-14|K|3.1 2.1;
  1cng|A|2018-09-12|K|3.1 2.1;
  1j85|A|2018-08-14|K|3.1 2.1;
  6emu|A|2018-07-22|K|3.1 2.1;
  5l0z|A|2018-06-12|K|3.1 2.1;
  5lle|A|2018-06-12|K|3.1 2.1;
  5llp|A|2018-06-12|K|3.1 2.1;
  5m4s|A|2018-06-12|K|3.1 2.1;
  5msb|A|2018-06-12|K|3.1 2.1;
  5nxo|A|2018-06-12|K|3.1 2.1;
  5nxp|A|2018-06-12|K|3.1 2.1;
  5ny1|A|2018-06-12|K|3.1 2.1;
  5ny6|A|2018-06-12|K|3.1 2.1;
  5oql|e|2018-06-12|K|3.1 2.1;
  5sz4|A|2018-06-12|K|3.1 2.1;
  1avn|A|2018-06-12|K|3.1 2.1;
  1k3r|A|2018-06-12|K|3.1 2.1;
  1ugf|A|2018-06-11|K|3.1 2.1;
  5fai|A|2018-06-11|K|3.1 2.1;
  1ipa|A|2018-06-11|K|3.1 2.1;
  1v2x|A|2018-06-11|K|3.1 2.1;
  1v6z|A|2018-06-11|K|3.1 2.1;
  2w2j|A|2018-06-11|K|3.1 2.1;
  1vh0|A|2018-06-11|K|3.1 2.1;
  1vhk|A|2018-06-11|K|3.1 2.1;
  1jv0|A|2018-06-11|K|3.1 2.1;
  4e8b|A|2018-06-11|K|3.1 2.1;
  1vhy|A|2018-06-11|K|3.1 2.1;
  4fak|A|2018-06-11|K|3.1 2.1;
  4fmw|A|2018-06-11|K|3.1 2.1;
  1x7o|A|2018-06-11|K|3.1 2.1;
  1x7p|A|2018-06-11|K|3.1 2.1;
  2wd2|A|2018-06-11|K|3.1 2.1;
  1xev|A|2018-06-11|K|3.1 2.1;
  3n4k|A|2018-06-11|K|3.1 2.1;
  5gm8|A|2018-06-11|K|3.1 2.1;
  5gmb|A|2018-06-11|K|3.1 2.1;
  1y7w|A|2018-06-11|K|3.1 2.1;
  5gmc|A|2018-06-11|K|3.1 2.1;
  2x7u|A|2018-06-11|K|3.1 2.1;
  3nk7|A|2018-06-11|K|3.1 2.1;
  5gra|A|2018-06-11|K|3.1 2.1;
  4h6v|A|2018-06-11|K|3.1 2.1;
  1yh1|A|2018-06-11|K|3.1 2.1;
  1mxi|A|2018-06-11|K|3.1 2.1;
  3o7b|A|2018-06-11|K|3.1 2.1;
  2yfk|A|2018-06-11|K|3.1 2.1;
  4riv|A|2018-06-11|K|3.1 2.1;
  2z0y|A|2018-06-11|K|3.1 2.1;
  4hpv|A|2018-06-11|K|3.1 2.1;
  3oij|A|2018-06-11|K|3.1 2.1;
  5h5e|A|2018-06-11|K|3.1 2.1;
  2znc|A|2018-06-11|K|3.1 2.1;
  5h5f|A|2018-06-11|K|3.1 2.1;
  1ns5|A|2018-06-11|K|3.1 2.1;
  1nxz|A|2018-06-11|K|3.1 2.1;
  3oin|A|2018-06-11|K|3.1 2.1;
  1o6d|A|2018-06-11|K|3.1 2.1;
  4ig6|A|2018-06-11|K|3.1 2.1;
  5hwy|A|2018-06-11|K|3.1 2.1;
  4twl|A|2018-06-11|K|3.1 2.1;
  3onp|A|2018-06-11|K|3.1 2.1;
  4twm|A|2018-06-11|K|3.1 2.1;
  3b1b|A|2018-06-11|K|3.1 2.1;
  3bbd|A|2018-06-11|K|3.1 2.1;
  3bbe|A|2018-06-11|K|3.1 2.1;
  3bet|A|2018-06-11|K|3.1 2.1;
  1zsa|A|2018-06-11|K|3.1 2.1;
  4jak|A|2018-06-11|K|3.1 2.1;
  4jal|A|2018-06-11|K|3.1 2.1;
  3c7p|A|2018-06-11|K|3.1 2.1;
  5jn3|A|2018-06-11|K|3.1 2.1;
  3q98|A|2018-06-11|K|3.1 2.1;
  4jwf|A|2018-06-11|K|3.1 2.1;
  5jpq|e|2018-06-11|K|3.1 2.1;
  4jwg|A|2018-06-11|K|3.1 2.1;
  4jwh|A|2018-06-11|K|3.1 2.1;
  4jwj|A|2018-06-11|K|3.1 2.1;
  4k0b|A|2018-06-11|K|3.1 2.1;
  3d93|A|2018-06-11|K|3.1 2.1;
  4ws9|A|2018-06-11|K|3.1 2.1;
  4k1c|A|2018-06-11|K|3.1 2.1;
  1rza|A|2018-06-11|K|3.1 2.1;
  3dcm|X|2018-06-11|K|3.1 2.1;
  4kdz|A|2018-06-11|K|3.1 2.1;
  1rzc|A|2018-06-11|K|3.1 2.1;
  4kgn|A|2018-06-11|K|3.1 2.1;
  5kzk|A|2018-06-11|K|3.1 2.1;
  1rzd|A|2018-06-11|K|3.1 2.1;
  4x3m|A|2018-06-11|K|3.1 2.1;
  4kjr|A|2018-06-11|K|3.1 2.1;
  1tbt|X|2018-06-11|K|3.1 2.1;
  4kpp|A|2018-06-11|K|3.1 2.1;
  3ryz|A|2018-06-11|K|3.1 2.1;
  3e5y|A|2018-06-11|K|3.1 2.1;
  3rz5|A|2018-06-11|K|3.1 2.1;
  3rz7|A|2018-06-11|K|3.1 2.1;
  4ktv|A|2018-06-11|K|3.1 2.1;
  3ed7|A|2018-06-11|K|3.1 2.1;
  3s76|A|2018-06-11|K|3.1 2.1;
  5nxg|A|2018-06-11|K|3.1 2.1;
  4ypx|A|2018-06-11|K|3.1 2.1;
  5ny3|A|2018-06-11|K|3.1 2.1;
  4l69|A|2018-06-11|K|3.1 2.1;
  3s97|A|2018-06-11|K|3.1 2.1;
  4l7i|A|2018-06-11|K|3.1 2.1;
  2cbe|A|2018-06-11|K|3.1 2.1;
  3sig|A|2018-06-11|K|3.1 2.1;
  2cx8|A|2018-06-11|K|3.1 2.1;
  2d1g|A|2018-06-11|K|3.1 2.1;
  3sij|A|2018-06-11|K|3.1 2.1;
  2egv|A|2018-06-11|K|3.1 2.1;
  4yqd|A|2018-06-11|K|3.1 2.1;
  2egw|A|2018-06-11|K|3.1 2.1;
  5sz0|A|2018-06-11|K|3.1 2.1;
  5sz1|A|2018-06-11|K|3.1 2.1;
  3gyq|A|2018-06-11|K|3.1 2.1;
  2fg6|C|2018-06-11|K|3.1 2.1;
  2fg7|C|2018-06-11|K|3.1 2.1;
  2fg7|X|2018-06-11|K|3.1 2.1;
  5t75|A|2018-06-11|K|3.1 2.1;
  4yr1|A|2018-06-11|K|3.1 2.1;
  4yvh|A|2018-06-11|K|3.1 2.1;
  2fos|A|2018-06-11|K|3.1 2.1;
  3iai|A|2018-06-11|K|3.1 2.1;
  4yvi|A|2018-06-11|K|3.1 2.1;
  3ibi|A|2018-06-11|K|3.1 2.1;
  4yvj|A|2018-06-11|K|3.1 2.1;
  4yvk|A|2018-06-11|K|3.1 2.1;
  3ibn|A|2018-06-11|K|3.1 2.1;
  1cra|A|2018-06-11|K|3.1 2.1;
  3ibu|A|2018-06-11|K|3.1 2.1;
  2g7m|C|2018-06-11|K|3.1 2.1;
  3ic6|A|2018-06-11|K|3.1 2.1;
  5tt8|A|2018-06-11|K|3.1 2.1;
  5tv3|A|2018-06-11|K|3.1 2.1;
  5twk|A|2018-06-11|K|3.1 2.1;
  3ilk|A|2018-06-11|K|3.1 2.1;
  2ha8|A|2018-06-11|K|3.1 2.1;
  5a7t|A|2018-06-11|K|3.1 2.1;
  5a7y|A|2018-06-11|K|3.1 2.1;
  2i6d|A|2018-06-11|K|3.1 2.1;
  5a7z|A|2018-06-11|K|3.1 2.1;
  3jyw|E|2018-06-11|K|3.1 2.1;
  3v5s|A|2018-06-11|K|3.1 2.1;
  3v5u|A|2018-06-11|K|3.1 2.1;
  5apg|A|2018-06-11|K|3.1 2.1;
  3knu|A|2018-06-11|K|3.1 2.1;
  5wyr|A|2018-06-11|K|3.1 2.1;
  5y2r|A|2018-06-11|K|3.1 2.1;
  3kty|A|2018-06-11|K|3.1 2.1;
  5c74|A|2018-06-11|K|3.1 2.1;
  1f48|A|2018-06-11|K|3.1 2.1;
  3kw2|A|2018-06-11|K|3.1 2.1;
  3ky7|A|2018-06-11|K|3.1 2.1;
  3kzc|A|2018-06-11|K|3.1 2.1;
  1fqn|A|2018-06-11|K|3.1 2.1;
  3kzk|A|2018-06-11|K|3.1 2.1;
  4o6d|A|2018-06-11|K|3.1 2.1;
  3kzm|A|2018-06-11|K|3.1 2.1;
  4o6d|B|2018-06-11|K|3.1 2.1;
  5cjl|A|2018-06-11|K|3.1 2.1;
  3kzn|A|2018-06-11|K|3.1 2.1;
  3kzo|A|2018-06-11|K|3.1 2.1;
  5co4|A|2018-06-11|K|3.1 2.1;
  3l02|A|2018-06-11|K|3.1 2.1;
  3l04|A|2018-06-11|K|3.1 2.1;
  1fug|A|2018-06-11|K|3.1 2.1;
  3l05|A|2018-06-11|K|3.1 2.1;
  3l06|A|2018-06-11|K|3.1 2.1;
  2nxt|A|2018-06-11|K|3.1 2.1;
  3l8u|A|2018-06-11|K|3.1 2.1;
  5doh|A|2018-06-11|K|3.1 2.1;
  5drs|A|2018-06-11|K|3.1 2.1;
  5dso|A|2018-06-11|K|3.1 2.1;
  4cnd|A|2018-06-11|K|3.1 2.1;
  5dsq|A|2018-06-11|K|3.1 2.1;
  4cnd|B|2018-06-11|K|3.1 2.1;
  5dsr|A|2018-06-11|K|3.1 2.1;
  1gz0|A|2018-06-11|K|3.1 2.1;
  4cne|A|2018-06-11|K|3.1 2.1;
  4cnf|A|2018-06-11|K|3.1 2.1;
  3m40|A|2018-06-11|K|3.1 2.1;
  4cng|A|2018-06-11|K|3.1 2.1;
  3m4j|A|2018-06-11|K|3.1 2.1;
  3m4n|A|2018-06-11|K|3.1 2.1;
  3m5c|A|2018-06-11|K|3.1 2.1;
  3m5d|A|2018-06-11|K|3.1 2.1;
  3m5e|A|2018-06-11|K|3.1 2.1;
  2qmm|A|2018-06-11|K|3.1 2.1;
  1hva|A|2018-06-11|K|3.1 2.1;
  4pzk|A|2018-06-11|K|3.1 2.1;
  2qwv|A|2018-06-11|K|3.1 2.1;
  1to0|A|2018-06-11|K|3.1 2.1;
  3m96|A|2018-06-11|K|3.1 2.1;
  3m98|A|2018-06-11|K|3.1 2.1;
  1uaj|A|2018-06-11|K|3.1 2.1;
  1ual|A|2018-06-11|K|3.1 2.1;
  1uam|A|2018-06-11|K|3.1 2.1;
  2v3j|A|2018-06-11|K|3.1 2.1;
  2v3k|A|2018-06-11|K|3.1 2.1;
  3mhi|A|2018-06-11|K|3.1 2.1;
  3mhm|A|2018-06-11|K|3.1 2.1;
  1by7|A|2018-06-10|K|3.1 2.1;

      
Knotoid types pdb Title
K 3.1, 2.1 6eeaA Bioreductive 4-hydroxy-3-nitro-5-ureido-benzenesulfonamides selectively target the tumor-associated carbonic anhydrase isoforms ix and xii and show hypoxia-enhanced cytotoxicity against human cancer cell lines.
K 3.1, 2.1 6ebeA Bioreductive 4-hydroxy-3-nitro-5-ureido-benzenesulfonamides selectively target the tumor-associated carbonic anhydrase isoforms ix and xii and show hypoxia-enhanced cytotoxicity against human cancer cell lines.
K 3.1, 2.1 6edaA Bioreductive 4-hydroxy-3-nitro-5-ureido-benzenesulfonamides selectively target the tumor-associated carbonic anhydrase isoforms ix and xii and show hypoxia-enhanced cytotoxicity against human cancer cell lines.
K 3.1, 2.1 6eeoA Bioreductive 4-hydroxy-3-nitro-5-ureido-benzenesulfonamides selectively target the tumor-associated carbonic anhydrase isoforms ix and xii and show hypoxia-enhanced cytotoxicity against human cancer cell lines.
K 3.1, 2.1 6eehA Bioreductive 4-hydroxy-3-nitro-5-ureido-benzenesulfonamides selectively target the tumor-associated carbonic anhydrase isoforms ix and xii and show hypoxia-enhanced cytotoxicity against human cancer cell lines.
K 3.1, 2.1 6eczA Bioreductive 4-hydroxy-3-nitro-5-ureido-benzenesulfonamides selectively target the tumor-associated carbonic anhydrase isoforms ix and xii and show hypoxia-enhanced cytotoxicity against human cancer cell lines.
K 3.1, 2.1
2
6g3qA Crystal structure of human carbonic anhydrase ii in complex with the inhibitor famotidine
K 3.1, 2.1 5thiA Crystal structure of 2-hydroxycyclohepta-2,4,6-trien-1-one bound to human carbonic anhydrase 2 l198g
K 3.1, 2.1 4knjA Crystal structure of human carbonic anhydrase isozyme ii with 2-chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide
K 3.1, 2.1 4qizA Crystal structure of human carbonic anhydrase isozyme xiii with inhibitor
K 3.1, 2.1 1bn1A Carbonic anhydrase ii inhibitor
K 3.1, 2.1 5n25A Crystal structure of human carbonic anhydrase ii in complex with the inhibitor 4-pyridin-3-yl-benzenesulfonamide
K 3.1, 2.1 5ohhA Crystal structure of human carbonic anhydrase isozyme xiii with 2-[(1s)-2,3-dihydro-1h-inden-1-ylamino]-3,5,6-trifluoro-4-[(2-hydroxyethyl)thio]benzenesulfonamide
K 3.1, 2.1 1cakA Structural analysis of the zinc hydroxide-thr 199-glu 106 hydrogen bonding network in human carbonic anhydrase ii
K 3.1, 2.1 1rzbA X-ray analysis of metal substituted human carbonic anhydrase ii derivatives
K 3.1, 2.1 4qsjA Crystal structure of human carbonic anhydrase isozyme xiii with 2-chloro-4-{[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)thio]acetyl}benzenesulfonamide
K 3.1, 2.1 1bv3A Human carbonic anhydrase ii complexed with urea
K 3.1, 2.1 1ttmA Human carbonic anhydrase ii complexed with 667-coumate
K 3.1, 2.1 5neaA Crystal structure of human carbonic anhydrase ii in complex with the inhibitor 4-(2-methyl-1,3-oxazol-5-yl)benzene-1-sulfonammide
K 3.1, 2.1 5fl5A Three dimensional structure of human carbonic anhydrase ix in complex with 5-(1-(4-methoxyphenyl)-1h-1,2,3-triazol-4-yl)thiophene-2- sulfonamide
K 3.1, 2.1 1bnnA Carbonic anhydrase ii inhibitor
K 3.1, 2.1 4yglA Naclo4--interactions between hofmeister anions and the binding pocket of a protein
K 3.1, 2.1 3iqkA Human carbonic anhydrase ii h64a complexed with thioxolone hydrolysis products
K 3.1, 2.1 6b59A Carbonic anhydrase ii in complex with nitrogenous base-bearing benezenesulfonamide
K 3.1, 2.1 3mnkA Human carbonic anhydrase ii mutant k170h
K 3.1, 2.1 1g3zA Carbonic anhydrase ii (f131v)
K 3.1, 2.1
2
2nnvA Structure of inhibitor binding to carbonic anhydrase ii
K 3.1, 2.1 3dc9A Use of carbonic anhydrase ii, ix active-site mimic, for the purpose of screening inhibitors for possible anti-cancer properties
K 3.1, 2.1 3dazA Use of carbonic anhydrase ii, ix active-site mimic, for the purpose of screening inhibitors for possible anti-cancer properties
K 3.1, 2.1 2cbaA Structure of native and apo carbonic anhydrase ii and some of its anion-ligand complexes
K 3.1, 2.1
2
3s72B The origin of the hydrophobic effect in the molecular recognition of arylsulfonamides by carbonic anhydrase
K 3.1, 2.1 2cbdA Structure of native and apo carbonic anhydrase ii and some of its anion-ligand complexes
K 3.1, 2.1 3nj9A Crystal structure of carbonic anhydrase ii in complex with a nir inhibitor
K 3.1, 2.1 4e3hA Nucleophile recognition as an alternative inhibition mode for benzoic acid based carbonic anhydrase inhibitors
K 3.1, 2.1 4ca2A Engineering the hydrophobic pocket of carbonic anhydrase ii
K 3.1, 2.1 4fptA Carbonic anhydrase ii in complex with ethyl (2z,4r)-2-(sulfamoylimino)-1,3-thiazolidine-4-carboxylate
K 3.1, 2.1 3r17B Hcarbonic anhydrase ii bound to n-(2-fluoro.4-sulfamoylphenyl)-2-(thiophen-2-yl) acetamide
K 3.1, 2.1 4zwzA Engineered carbonic anhydrase ix mimic in complex with a glucosyl sulfamate inhibitor
K 3.1, 2.1 4q07A Crystal structure of chimeric carbonic anhydrase ix with inhibitor
K 3.1, 2.1 5g01A An unusual natural product primary sulfonamide: synthesis, carbonic anhydrase inhibition and protein x-ray structure of psammaplin c
K 3.1, 2.1 4mdlA Meta carborane carbonic anhydrase inhibitor
K 3.1, 2.1
2
5tt3A Crystal structure of the complex of helicobacter pylori alpha-carbonic anhydrase with ethoxzolamide
K 3.1, 2.1 5umcA Synthesis of novel seleno ureido containing compounds as slc-0111 analogs. investigations on carbonic anhydrases activity, glutathione peroxidase and x-ray crystallography
K 3.1, 2.1 4q09A Crystal structure of chimeric carbonic anhydrase xii with inhibitor
K 3.1, 2.1 1g46A Carbonic anhydrase ii (f131v) complexed with 4-(aminosulfonyl)-n-[(2,3-difluorophenyl)methyl]-benzamide
K 3.1, 2.1 5ogpA Metalacarborane inhibitors of carbonic anhydrase ix
K 3.1, 2.1 1if6A Carbonic anhydrase ii complexed with 3,5-difluorobenzenesulfonamide
K 3.1, 2.1 6ekiA Structure of a hyperthermostable carbonic anhydrase identified from an active hydrothermal vent chimney
K 3.1, 2.1 3igpA Structure of inhibitor binding to carbonic anhydrase ii
K 3.1, 2.1 5fnhA Native state mass spectrometry, surface plasmon resonance and x-ray crystallography correlate strongly as a fragment screening combination
K 3.1, 2.1 3w6hA Crystal structure of 19f probe-labeled hcai in complex with acetazolamide
K 3.1, 2.1 5cluA The crystal structure of the complex of hcaii with a saccharine derivative
K 3.1, 2.1 1i9nA Carbonic anhydrase ii (f131v) complexed with 4-(aminosulfonyl)-n-[(2,5-difluorophenyl)methyl]-benzamide
K 3.1, 2.1 3mhcA Crystal structure of human cabonic anhydrase ii in adduct with an adamantyl analogue of acetazolamide in a novel hydrophobic binding pocket
K 3.1, 2.1 5flsA Native state mass spectrometry, surface plasmon resonance and x-ray crystallography correlate strongly as a fragment screening combination
K 3.1, 2.1 1cnjA X-ray crystallographic studies of engineered hydrogen bond networks in a protein-zinc binding site
K 3.1, 2.1 1if4A Carbonic anhydrase ii complexed with 4-fluorobenzenesulfonamide
K 3.1, 2.1 4k0tA Structure of hcaix mimic (hcaii with 5 mutations in active site) in complex with chlorzolamide
K 3.1, 2.1 4qsbA Crystal structure of human carbonic anhydrase isozyme ii with 3-{[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)thio]acetyl}benzenesulfonamide
K 3.1, 2.1 4k0sA Structure of hcaix mimic (hcaii with 5 mutations in active site) in complex with acetazolamide
K 3.1, 2.1 3mnaA The crystal structure of human carbonic anhydrase ii in complex with a 1,3,5-triazine-substituted benzenesulfonamide inhibitor
K 3.1, 2.1 4n0xB Room temperature crystal structure of human carbonic anhydrase ii in complex with thiophene-2-sulfonamide
K 3.1, 2.1 3mzcA Human carbonic ahydrase ii in complex with a benzenesulfonamide inhibitor
K 3.1, 2.1 5msaA Crystal structure of human carbonic anhydrase isozyme xii with 2,3,5,6-tetrafluoro-4-(propylthio)benzenesulfonamide
K 3.1, 2.1
2
5neeA Crystal structure of human carbonic anhydrase ii in complex with the inhibitor 5-[2-(morpholine-4-carbonyl)1,3-oxazol-5-yl)]thiophene-2-sulfonammide
K 3.1, 2.1 2hfwA Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase iii
K 3.1, 2.1 2f14A Tne crystal structure of the human carbonic anhydrase ii in complex with a fluorescent inhibitor
K 3.1, 2.1 3d92A Human carbonic anhydrase ii bound with substrate carbon dioxide
K 3.1, 2.1 4m2rA Human carbonic anhydrase ii in complex with brinzolamide
K 3.1, 2.1 5ljqA Crystal structure of human carbonic anhydrase ii in complex with the 4-(4-(phenoxymethyl)-1h-1,2,3-triazol-1-yl)benzenesulfonamide inhibitor
K 3.1, 2.1 3konA Crystal structure of cobalt (ii) human carbonic anhydrase ii at ph 11.0
K 3.1, 2.1 4qk2A Structural and catalytic effects of proline substitution and surface loop deletion in the extended active site of human carbonic anhydrase ii - e234p
K 3.1, 2.1 4z0qA Carbonic anhydrase inhibitors: design and synthesis of new heteroaryl-n-carbonylbenzenesulfonamides targeting druggable human carbonic anhydrase isoforms (hca vii, hca ix, and hca xiv)
K 3.1, 2.1 6fe2A Three dimensional structure of human carbonic anhydrase ix
K 3.1, 2.1 4gl1X Structure of h64a/n62l/n67l human carbonic anhydrase ii triple mutant
K 3.1, 2.1 2nwoA Structural and kinetic effect of hydrophobic mutations in the active site of human carbonic anhydrase ii
K 3.1, 2.1 1th9A Effect of shuttle location and ph environment on h+ transfer in human carbonic anhydrase ii
K 3.1, 2.1 1caoA Crystallographic studies of the binding of protonated and unprotonated inhibitors to carbonic anhydrase using hydrogen sulphide and nitrate anions
K 3.1, 2.1 4bf1A Three dimensional structure of human carbonic anhydrase ii in complex with 5-(1-naphthalen-1-yl-1,2,3-triazol-4-yl)thiophene-2-sulfonamide
K 3.1, 2.1 3dc3A Use of carbonic anhydrase ii, ix active-site mimic, for the purpose of screening inhibitors for possible anti-cancer properties
K 3.1, 2.1
2
2nnoA Structure of inhibitor binding to carbonic anhydrase ii
K 3.1, 2.1 4qj0A Crystal structure of catalytic domain of human carbonic anhydrase isozyme xii with inhibitor
K 3.1, 2.1 4cnvA Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion co2 capture
K 3.1, 2.1 4r59A A carbonic anhydrase ix mimic in complex with a carbohydrate-based sulfamate
K 3.1, 2.1 4mltA Structure of a monodentate 3-hydroxy-4h-pyran-4-thione ligand bound to hcaii
K 3.1, 2.1 3mnuA Carbonic anhydrase inhibitors: crystallographic and solution binding studies for the interaction of a boron containing aromatic sulfamide with mammalian isoforms i-xv
K 3.1, 2.1 3s75B The origin of the hydrophobic effect in the molecular recognition of arylsulfonamides by carbonic anhydrase
K 3.1, 2.1 4mdgA Closo carborane carbonic anhydrase inhibitor
K 3.1, 2.1 5eijA Carbonic anhydrase ii in complex with sulfonamide inhibitor
K 3.1, 2.1 3v2jA Effect of sucrose and glycerol as cryoprotectans, on the inhibition of human carbonic anhydrase ii
K 3.1, 2.1 3ml5A Crystal structure of the c183s/c217s mutant of human ca vii in complex with acetazolamide
K 3.1, 2.1 1cniA X-ray crystallographic studies of engineered hydrogen bond networks in a protein-zinc binding site
K 3.1, 2.1 2hocA Crystal structure of the human carbonic anhydrase ii in complex with the 5-(4-amino-3-chloro-5-fluorophenylsulfonamido)-1,3,4-thiadiazole-2-sulfonamide inhibitor
K 3.1, 2.1 4yxiA Human carbonic anhydrase ii complexed with an inhibitor with a benzenesulfonamide group (2).
K 3.1, 2.1 5fnlA Native state mass spectrometry, surface plasmon resonance and x-ray crystallography correlate strongly as a fragment screening combination
K 3.1, 2.1 4xz5A Structure of the thermostable alpha-carbonic anydrase from thiomicrospira crunogena xcl-2 gammaproteobacterium
K 3.1, 2.1 4q7pA Crystal structure of 1-hydroxy-3-methylpyridine-2(1h)-thione bound to hcaii
K 3.1, 2.1 5flrA Native state mass spectrometry, surface plasmon resonance and x-ray crystallography correlate strongly as a fragment screening combination
K 3.1, 2.1 5flpA Native state mass spectrometry, surface plasmon resonance and x-ray crystallography correlate strongly as a fragment screening combination
K 3.1, 2.1 4k0zA Structure of hcaix mimic (hcaii with 5 mutations in active site) in complex with methazolamide
K 3.1, 2.1 5e2sA Crystal structure of human carbonic anhydrase ii in complex with the 4-(2-iso-propylphenyl)benzenesulfonamide inhibitor
K 3.1, 2.1 2gd8A Crystal structure analysis of the human carbonic anhydrase ii in complex with a 2-substituted estradiol bis-sulfamate
K 3.1, 2.1 6equA X-ray crystal structure of the human carbonic anhydrase ii adduct with a membrane-impermeant inhibitor
K 3.1, 2.1
2
5jgsB Human carbonic anhydrase ii (f131y/l198a) complexed with benzo[d]thiazole-2-sulfonamide
K 3.1, 2.1 5fnjA Native state mass spectrometry, surface plasmon resonance and x-ray crystallography correlate strongly as a fragment screening combination
K 3.1, 2.1 1lgdA Crystal structure analysis of hca ii mutant t199p in complex with bicarbonate
K 3.1, 2.1 4ygnA Nai--interactions between hofmeister anions and the binding pocket of a protein
K 3.1, 2.1 4z1nA Carbonic anhydrase inhibitors: design and synthesis of new heteroaryl-n-carbonylbenzenesulfonamides targeting druggable human carbonic anhydrase isoforms (hca vii, hca ix, and hca xiv)
K 3.1, 2.1
2
3fe4A Crystal structure of human carbonic anhydrase vi
K 3.1, 2.1 5lmdA The crystal structure of hca ii in complex with a benzoxaborole inhibitor
K 3.1, 2.1 1ze8A Carbonic anhydrase ii in complex with a membrane-impermeant sulfonamide inhibitor
K 3.1, 2.1 4k13A Structure of hcaix mimic (hcaii with 5 mutations in active site) in complex with dorzolamide
K 3.1, 2.1 3ryjB Carbonic anhydrase complexed with 4-sulfamoyl-n-(2,2,2-trifluoroethyl)benzamide
K 3.1, 2.1 1te3X Effect of shuttle location and ph environment on h+ transfer in human carbonic anhydrase ii
K 3.1, 2.1 3rz1B Fluoroalkyl and alkyl chains have similar hydrophobicities in binding to the hydrophobic wall of carbonic anhydrase
K 3.1, 2.1 5sz5A Carbonic anhydrase ix-mimic in complex with 4-(2-methylphenyl)-benzenesulfonamide
K 3.1, 2.1 1fqlA X-ray crystal structure of zinc-bound f95m/w97v carbonic anhydrase (caii) variant
K 3.1, 2.1 1z97A Human carbonic anhydrase iii: structural and kinetic study of catalysis and proton transfer.
K 3.1, 2.1 5cjfA The crystal structure of the human carbonic anhydrase xiv in complex with a 1,1'-biphenyl-4-sulfonamide inhibitor.
K 3.1, 2.1 5txyA Identification of a new zinc binding chemotype of by fragment screening on human carbonic anhydrase
K 3.1, 2.1 1fsqA X-ray crystal structure of cobalt-bound f93s/f95l/w97m carbonic anhydrase (caii) variant
K 3.1, 2.1 4q49A Room temperature neutron crystal structure of apo human carbonic anhydrase at ph 7.5
K 3.1, 2.1 1bn4A Carbonic anhydrase ii inhibitor
K 3.1, 2.1 5bu6B Structure of bpsb deaceylase domain from bordetella bronchiseptica
K 3.1, 2.1 3ryvB Carbonic anhydrase complexed with n-ethyl-4-sulfamoylbenzamide
K 3.1, 2.1
2
2foqA Human carbonic anhydrase ii complexed with two-prong inhibitors
K 3.1, 2.1 5th4A Crystal structure of 1-hydroxypyridine-2(1h)-thione bound to human carbonic anhydrase 2 l198g
K 3.1, 2.1 1yo0A Proton transfer from his200 in human carbonic anhydrase ii
K 3.1, 2.1 5floA Native state mass spectrometry, surface plasmon resonance and x-ray crystallography correlate strongly as a fragment screening combination
K 3.1, 2.1 4qk1A Structural and catalytic effects of proline substitution and surface loop deletion in the extended active site of human carbonic anhydrase ii - k170p
K 3.1, 2.1 3gz0A Apo-human carbonic anhydrase ii revisited: implications of the loss of a metal in protein structure, stability and solvent network
K 3.1, 2.1 5jesB Human carbonic anhydrase ii (v121t) complexed with benzo[d]thiazole-2-sulfonamide
K 3.1, 2.1 6b5aA Carbonic anhydrase ix-mimic in complex with nitrogenous base-bearing benezenesulfonamide
K 3.1, 2.1
2
2nngA Structure of inhibitor binding to carbonic anhydrase ii
K 3.1, 2.1 3p3jA Human carbonic anhydrase ii in complex with p-(5-ruthenocenyl-1h-1,2,3-triazol-1-yl)benzenesulfonamide
K 3.1, 2.1 5fdiA Crystal structure of human carbonic anhydrase ii with the anticonvulsant sulfamide jnj-26990990 and its s,s-dioxide analog.
K 3.1, 2.1 3mniA Human carbonic anhydrase ii mutant k170d
K 3.1, 2.1 1ugdA Human carbonic anhydrase ii[hcaii] (e.c.4.2.1.1) mutant with ala 65 replaced by ser (a65s)
K 3.1, 2.1
2
2x7sA Structures of human carbonic anhydrase ii inhibitor complexes reveal a second binding site for steroidal and non-steroidal inhibitors.
K 3.1, 2.1 2fnnA Activation of human carbonic anhydrase ii by exogenous proton donors
K 3.1, 2.1
4
5jdfA Structural mechanisms of extracellular ion exchange and induced binding-site occlusion in the sodium-calcium exchanger ncx_mj soaked with 2.5 mm na+ and 1mm ca2+
K 3.1, 2.1 3mnjA Human carbonic anhydrase ii mutant k170e
K 3.1, 2.1 3hljA Crystal structure of human carbonic anhydrase isozyme ii with 3-methylthiobenzimidazo[1,2-c][1,2,3]thiadiazol-7-sulfonamide
K 3.1, 2.1 3oikA Human carbonic anhydrase ii mutant a65s, n67q (ca ix mimic) bound by 2-ethylestradiol 3,17-o,o-bis-sulfamate
K 3.1, 2.1 3hknA Human carbonic anhydrase ii in complex with (2,3,4,6-tetra-o-acetyl-beta-d-galactopyranosyl) -(1-4)-1,2,3,6-tetra-o-acetyl-1-thio-beta-d-glucopyranosylsulfonamide
K 3.1, 2.1 3u3aX Structure of human carbonic anhydrase ii v143i
K 3.1, 2.1 4qk3A Structural and catalytic effects of proline substitution and surface loop deletion in the extended active site of human carbonic anhydrase ii - [delta]230-240
K 3.1, 2.1 4kp5A Crystal structure of catalytic domain of human carbonic anhydrase isozyme xii with 2-chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide
K 3.1, 2.1 5jepB Human carbonic anhydrase ii (t199s) complexed with benzo[d]thiazole-2-sulfonamide
K 3.1, 2.1 4rn4A Human carbonic anhydrases ii in complex with a acetazolamide derivative comprising one hydrophobic and one hydrophilic tail moiety

KnotProt | Interdisciplinary Laboratory of Biological Systems Modelling