KnotProt 2.0: A database of proteins with knots and slipknots

Found 691 chains in Knotted chains table. Displaying 451 - 600. Applied filters: Probabilistic

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Knots
Knotoids

Search results query ec: 4.2.1.1

#pdbid|chain|deposition date|is S/K-not|(slip)knot types;
      
  7ng1|A|2022-07-25|K|+3.1;
  7mu3|A|2021-10-04|K|+3.1;
  6zr9|A|2021-06-23|K|+3.1;
  6rrg|A|2021-05-24|K|+3.1;
  6yj3|A|2020-09-16|K|+3.1;
  6yok|A|2020-09-01|K|+3.1;
  6y74|A|2020-08-23|K|+3.1;
  6yma|A|2020-08-23|K|+3.1;
  6ymb|A|2020-08-23|S|+3.1;
  6ufd|A|2020-08-22|S|+3.1;
  6ufb|A|2020-08-22|S|+3.1;
  6ufc|A|2020-08-22|S|+3.1;
  6klz|A|2020-08-20|S|+3.1;
  6km0|A|2020-08-20|S|+3.1;
  6km1|A|2020-08-20|K|+3.1;
  6km2|A|2020-08-20|K|+3.1;
  6km3|A|2020-08-20|K|+3.1;
  6km4|A|2020-08-20|S|+3.1;
  6km5|A|2020-08-20|K|+3.1;
  6km6|A|2020-08-20|S|+3.1;
  6wq7|A|2020-08-06|K|+3.1;
  6wq4|A|2020-08-06|S|+3.1;
  6wq8|A|2020-08-06|S|+3.1;
  6wq9|A|2020-08-06|S|+3.1;
  6t7u|A|2020-08-05|S|+3.1;
  6t9z|A|2020-08-05|S|+3.1;
  6rmx|A|2020-08-05|S|+3.1;
  6otk|A|2020-08-04|S|+3.1;
  6oto|A|2020-08-04|S|+3.1;
  6otm|A|2020-08-04|K|+3.1;
  6oti|A|2020-08-04|K|+3.1;
  6otq|A|2020-08-04|S|+3.1;
  6oub|A|2020-08-04|S|+3.1;
  6otp|A|2020-08-04|S|+3.1;
  6ouh|A|2020-08-04|S|+3.1;
  6oud|A|2020-08-04|S|+3.1;
  6ouf|A|2020-08-04|S|+3.1;
  6ouk|A|2020-08-04|S|+3.1;
  6oui|A|2020-08-04|S|+3.1;
  6ouj|A|2020-08-04|S|+3.1;
  6oum|A|2020-08-04|S|+3.1;
  6oue|A|2020-08-04|K|+3.1;
  6rg4|A|2020-08-04|K|+3.1;
  6rg3|A|2020-08-04|S|+3.1;
  6rhj|A|2020-08-04|K|+3.1;
  6rmy|A|2020-08-04|S|+3.1;
  6rof|A|2020-08-04|K|+3.1;
  6rhk|A|2020-08-04|S|+3.1;
  6rzx|A|2020-08-04|S|+3.1;
  6s03|A|2020-08-04|S|+3.1;
  6sds|A|2020-08-04|S|+3.1;
  6sdt|A|2020-08-04|S|+3.1;
  6ux1|A|2020-04-30|K|+3.1;
  6r6j|A|2020-04-17|S|+3.1;
  6r6y|A|2020-04-17|K|+3.1;
  6r71|A|2020-04-17|S|+3.1;
  6qut|A|2020-04-07|S|+3.1;
  6vj3|A|2020-04-02|K|+3.1;
  6ugr|A|2020-03-31|S|+3.1;
  6ugp|A|2020-03-31|S|+3.1;
  6ugz|A|2020-03-31|S|+3.1;
  6ugq|A|2020-03-31|S|+3.1;
  6ugn|A|2020-03-31|K|+3.1;
  6ugo|A|2020-03-31|S|+3.1;
  6uh0|A|2020-03-31|S|+3.1;
  6pdv|A|2020-03-30|S|+3.1;
  6r6f|A|2020-03-30|S|+3.1;
  6qng|A|2020-03-30|K|+3.1;
  6qnl|A|2020-03-30|K|+3.1;
  6pea|A|2020-03-30|S|+3.1;
  6qn0|A|2020-03-08|S|+3.1;
  6qn2|A|2020-03-08|S|+3.1;
  6qn5|A|2020-03-08|K|+3.1;
  6qn6|A|2020-03-08|S|+3.1;
  6u4q|A|2020-01-29|S|+3.1;
  6u4t|A|2020-01-29|S|+3.1;
  6nm0|A|2020-01-22|S|+3.1;
  6nlv|A|2020-01-22|S|+3.1;
  6i0l|A|2019-11-27|S|+3.1;
  6i0j|A|2019-11-27|K|+3.1;
  6i1u|A|2019-11-27|S|+3.1;
  6i2f|A|2019-11-27|S|+3.1;
  6i0w|A|2019-11-27|K|+3.1;
  6qqm|A|2019-11-15|K|+3.1;
  6hxd|A|2019-11-07|S|+3.1;
  6hr3|A|2019-10-18|K|+3.1;
  6nj2|A|2019-10-17|K|+3.1;
  6nj3|A|2019-10-17|S|+3.1;
  6nj6|A|2019-10-17|S|+3.1;
  6nj5|A|2019-10-17|K|+3.1;
  6nj4|A|2019-10-17|K|+3.1;
  6ql1|A|2019-10-16|S|+3.1;
  6ql2|A|2019-10-16|S|+3.1;
  6ql3|A|2019-10-16|K|+3.1;
  6hzx|A|2019-09-25|K|+3.1;
  6rqq|A|2019-09-21|K|+3.1;
  6rqn|A|2019-09-21|K|+3.1;
  6hd2|A|2019-09-11|S|+3.1;
  12ca|A|2018-10-21|S|+3.1;
  1azm|A|2018-10-21|S|+3.1;
  1bnn|A|2018-10-21|S|+3.1;
  1bv3|A|2018-10-21|S|+3.1;
  1cak|A|2018-10-21|K|+3.1;
  1rzb|A|2018-10-21|S|+3.1;
  1ttm|A|2018-10-21|S|+3.1;
  4qsj|A|2018-10-21|S|+3.1;
  4ygl|A|2018-10-21|S|+3.1;
  4qiz|A|2018-10-21|S|+3.1;
  5fl5|A|2018-10-21|K|+3.1;
  1bn1|A|2018-10-20|S|+3.1;
  1bn3|A|2018-10-20|S|+3.1;
  1bn4|A|2018-10-20|S|+3.1;
  1bnq|A|2018-10-20|S|+3.1;
  1cao|A|2018-10-20|K|+3.1;
  1ccs|A|2018-10-20|S|+3.1;
  1cni|A|2018-10-20|S|+3.1;
  1cnj|A|2018-10-20|K|+3.1;
  1cvb|A|2018-10-20|S|+3.1;
  1cve|A|2018-10-20|S|+3.1;
  1fql|A|2018-10-20|S|+3.1;
  1fsq|A|2018-10-20|K|+3.1;
  1g3z|A|2018-10-20|S|+3.1;
  1g46|A|2018-10-20|S|+3.1;
  1hcb|A|2018-10-20|S|+3.1;
  1hea|A|2018-10-20|S|+3.1;
  1hug|A|2018-10-20|S|+3.1;
  1huh|A|2018-10-20|S|+3.1;
  1i9n|A|2018-10-20|S|+3.1;
  1if4|A|2018-10-20|S|+3.1;
  1if6|A|2018-10-20|S|+3.1;
  1j9w|A|2018-10-20|S|+3.1;
  1lgd|A|2018-10-20|S|+3.1;
  1rj5|A|2018-10-20|S|+3.1;
  1te3|X|2018-10-20|S|+3.1;
  1th9|A|2018-10-20|S|+3.1;
  1ugd|A|2018-10-20|K|+3.1;
  1ydd|A|2018-10-20|S|+3.1;
  1yo0|A|2018-10-20|S|+3.1;
  1z97|A|2018-10-20|K|+3.1;
  1ze8|A|2018-10-20|K|+3.1;
  1zsc|A|2018-10-20|S|+3.1;
  2cba|A|2018-10-20|S|+3.1;
  2cbd|A|2018-10-20|S|+3.1;
  2eu3|A|2018-10-20|S|+3.1;
  2f14|A|2018-10-20|S|+3.1;
  2fnn|A|2018-10-20|K|+3.1;
  2foq|A|2018-10-20|S|+3.1;
  2fw4|A|2018-10-20|S|+3.1;
  2gd8|A|2018-10-20|S|+3.1;
  2hfw|A|2018-10-20|S|+3.1;
  2hoc|A|2018-10-20|S|+3.1;
  2nng|A|2018-10-20|S|+3.1;
  2nno|A|2018-10-20|K|+3.1;
  2nnv|A|2018-10-20|S|+3.1;
  2nwo|A|2018-10-20|K|+3.1;
  2vvb|X|2018-10-20|K|+3.1;
  2weh|A|2018-10-20|S|+3.1;
  2x7s|A|2018-10-20|S|+3.1;
  3bl1|A|2018-10-20|S|+3.1;
  3d92|A|2018-10-20|S|+3.1;
  3daz|A|2018-10-20|K|+3.1;
  3dc3|A|2018-10-20|S|+3.1;
  3dc9|A|2018-10-20|S|+3.1;
  3f4x|A|2018-10-20|S|+3.1;
  3fe4|A|2018-10-20|S|+3.1;
  3gz0|A|2018-10-20|K|+3.1;
  3hkn|A|2018-10-20|K|+3.1;
  3hlj|A|2018-10-20|S|+3.1;
  3ieo|A|2018-10-20|S|+3.1;
  3igp|A|2018-10-20|S|+3.1;
  3kkx|A|2018-10-20|K|+3.1;
  3kon|A|2018-10-20|K|+3.1;
  3mhc|A|2018-10-20|K|+3.1;
  3ml5|A|2018-10-20|K|+3.1;
  3mni|A|2018-10-20|S|+3.1;
  3mnj|A|2018-10-20|S|+3.1;
  3mnk|A|2018-10-20|S|+3.1;
  3mnu|A|2018-10-20|K|+3.1;
  3mwo|A|2018-10-20|S|+3.1;
  3mzc|A|2018-10-20|S|+3.1;
  4ca2|A|2018-10-20|S|+3.1;
  4g7a|A|2018-10-20|S|+3.1;
  4gl1|X|2018-10-20|S|+3.1;
  4m2w|A|2018-10-20|S|+3.1;
  7ca2|A|2018-10-20|S|+3.1;
  3oik|A|2018-10-20|S|+3.1;
  3nj9|A|2018-10-20|S|+3.1;
  3mna|A|2018-10-20|S|+3.1;
  3u3a|X|2018-10-20|K|+3.1;
  3v2j|A|2018-10-20|K|+3.1;
  4n0x|B|2018-10-20|S|+3.1;
  4mty|A|2018-10-20|S|+3.1;
  4mdg|A|2018-10-20|K|+3.1;
  4mdl|A|2018-10-20|K|+3.1;
  4m2r|A|2018-10-20|K|+3.1;
  4knj|A|2018-10-20|S|+3.1;
  4fpt|A|2018-10-20|K|+3.1;
  3p3j|A|2018-10-20|K|+3.1;
  4e3h|A|2018-10-20|S|+3.1;
  4bf1|A|2018-10-20|S|+3.1;
  4bcw|A|2018-10-20|S|+3.1;
  3ryv|B|2018-10-20|S|+3.1;
  3ryj|B|2018-10-20|K|+3.1;
  3r17|B|2018-10-20|S|+3.1;
  3p44|A|2018-10-20|S|+3.1;
  4l5v|A|2018-10-20|K|+3.1;
  4k13|A|2018-10-20|S|+3.1;
  4k0z|A|2018-10-20|S|+3.1;
  4k0t|A|2018-10-20|S|+3.1;
  4k0s|A|2018-10-20|S|+3.1;
  4mlt|A|2018-10-20|K|+3.1;
  3s75|B|2018-10-20|S|+3.1;
  3s72|B|2018-10-20|K|+3.1;
  3rz1|B|2018-10-20|S|+3.1;
  4kp5|A|2018-10-20|K|+3.1;
  3w6i|A|2018-10-20|S|+3.1;
  3w6h|A|2018-10-20|S|+3.1;
  4pq7|A|2018-10-20|S|+3.1;
  4r59|A|2018-10-20|K|+3.1;
  4cnv|A|2018-10-20|S|+3.1;
  4rn4|A|2018-10-20|S|+3.1;
  4q09|A|2018-10-20|S|+3.1;
  4pyy|A|2018-10-20|S|+3.1;
  4q08|A|2018-10-20|S|+3.1;
  4q07|A|2018-10-20|S|+3.1;
  4qsb|A|2018-10-20|K|+3.1;
  4ygn|A|2018-10-20|K|+3.1;
  4ywp|A|2018-10-20|K|+3.1;
  4z0q|A|2018-10-20|S|+3.1;
  5clu|A|2018-10-20|S|+3.1;
  4qk2|A|2018-10-20|S|+3.1;
  4qk1|A|2018-10-20|K|+3.1;
  4qj0|A|2018-10-20|S|+3.1;
  4z1e|A|2018-10-20|K|+3.1;
  4q7p|A|2018-10-20|S|+3.1;
  4z1n|A|2018-10-20|S|+3.1;
  4q49|A|2018-10-20|S|+3.1;
  4zwz|A|2018-10-20|S|+3.1;
  4xe1|A|2018-10-20|S|+3.1;
  4qk3|A|2018-10-20|S|+3.1;
  5cjf|A|2018-10-20|K|+3.1;
  4xz5|A|2018-10-20|K|+3.1;
  1am6|A|2018-10-19|S|+3.1;
  1bnt|A|2018-10-19|S|+3.1;
  1bnu|A|2018-10-19|S|+3.1;
  1bnw|A|2018-10-19|S|+3.1;
  1bzm|A|2018-10-19|S|+3.1;
  1cah|A|2018-10-19|S|+3.1;
  1cai|A|2018-10-19|S|+3.1;
  1cal|A|2018-10-19|S|+3.1;
  1cay|A|2018-10-19|S|+3.1;
  1caz|A|2018-10-19|S|+3.1;
  1cct|A|2018-10-19|S|+3.1;
  1cvh|A|2018-10-19|S|+3.1;
  1dca|A|2018-10-19|S|+3.1;
  1dcb|A|2018-10-19|S|+3.1;
  1eou|A|2018-10-19|S|+3.1;
  1fqr|A|2018-10-19|S|+3.1;
  1fr4|A|2018-10-19|S|+3.1;
  1g0f|A|2018-10-19|K|+3.1;
  1g45|A|2018-10-19|S|+3.1;
  1g48|A|2018-10-19|S|+3.1;
  1g53|A|2018-10-19|S|+3.1;
  1g6v|A|2018-10-19|S|+3.1;
  1h9n|A|2018-10-19|S|+3.1;
  1koq|A|2018-10-19|S|+3.1;
  1mua|A|2018-10-19|S|+3.1;
  1okm|A|2018-10-19|S|+3.1;
  1okn|A|2018-10-19|S|+3.1;
  1oq5|A|2018-10-19|S|+3.1;
  1ray|A|2018-10-19|S|+3.1;
  1raz|A|2018-10-19|K|+3.1;
  1rj6|A|2018-10-19|S|+3.1;
  1t9n|A|2018-10-19|S|+3.1;
  1uga|A|2018-10-19|S|+3.1;
  1v9i|C|2018-10-19|S|+3.1;
  1xq0|A|2018-10-19|S|+3.1;
  1zsb|A|2018-10-19|S|+3.1;
  2cab|A|2018-10-19|S|+3.1;
  2eu2|A|2018-10-19|K|+3.1;
  2fmz|A|2018-10-19|S|+3.1;
  2fnk|A|2018-10-19|K|+3.1;
  2fnm|A|2018-10-19|K|+3.1;
  2hnc|A|2018-10-19|S|+3.1;
  2it4|A|2018-10-19|S|+3.1;
  2nns|A|2018-10-19|K|+3.1;
  2pou|A|2018-10-19|K|+3.1;
  2pov|A|2018-10-19|S|+3.1;
  2q1b|A|2018-10-19|S|+3.1;
  2vva|X|2018-10-19|S|+3.1;
  2wd3|A|2018-10-19|K|+3.1;
  3dcs|A|2018-10-19|S|+3.1;
  3dcw|A|2018-10-19|S|+3.1;
  3dd0|A|2018-10-19|S|+3.1;
  3dv7|A|2018-10-19|K|+3.1;
  3dvd|A|2018-10-19|S|+3.1;
  3hkq|A|2018-10-19|S|+3.1;
  3hku|A|2018-10-19|S|+3.1;
  3hs4|A|2018-10-19|S|+3.1;
  3k7k|A|2018-10-19|S|+3.1;
  3ks3|A|2018-10-19|S|+3.1;
  3m1j|A|2018-10-19|S|+3.1;
  3myq|A|2018-10-19|K|+3.1;
  3n0n|A|2018-10-19|K|+3.1;
  3n2p|A|2018-10-19|S|+3.1;
  3v3h|B|2018-10-19|S|+3.1;
  3v3i|B|2018-10-19|S|+3.1;
  3v3j|A|2018-10-19|S|+3.1;
  4ht2|A|2018-10-19|K|+3.1;
  4jsa|A|2018-10-19|S|+3.1;
  4jsz|A|2018-10-19|S|+3.1;
  5ca2|A|2018-10-19|S|+3.1;
  5cac|A|2018-10-19|S|+3.1;
  3mmf|A|2018-10-19|S|+3.1;
  3m2z|A|2018-10-19|S|+3.1;
  3t5z|A|2018-10-19|S|+3.1;
  3t82|A|2018-10-19|S|+3.1;
  3v2m|A|2018-10-19|K|+3.1;
  3v7x|A|2018-10-19|K|+3.1;
  3m5t|A|2018-10-19|S|+3.1;
  3m1q|A|2018-10-19|K|+3.1;
  4mo8|A|2018-10-19|S|+3.1;
  4mdm|A|2018-10-19|K|+3.1;
  4m2u|A|2018-10-19|K|+3.1;
  4kni|A|2018-10-19|S|+3.1;
  4jss|A|2018-10-19|S|+3.1;
  4js6|A|2018-10-19|S|+3.1;
  4iwz|A|2018-10-19|K|+3.1;
  4ilx|A|2018-10-19|S|+3.1;
  4ito|A|2018-10-19|S|+3.1;
  4idr|X|2018-10-19|S|+3.1;
  4hey|A|2018-10-19|S|+3.1;
  4g0c|A|2018-10-19|S|+3.1;
  4fvn|A|2018-10-19|S|+3.1;
  4frc|A|2018-10-19|S|+3.1;
  4fl7|A|2018-10-19|K|+3.1;
  3oyq|A|2018-10-19|S|+3.1;
  3ni5|A|2018-10-19|S|+3.1;
  4e5q|A|2018-10-19|K|+3.1;
  4e4a|A|2018-10-19|K|+3.1;
  4e3f|A|2018-10-19|K|+3.1;
  4e3d|A|2018-10-19|S|+3.1;
  4dz7|A|2018-10-19|S|+3.1;
  3vbd|A|2018-10-19|K|+3.1;
  3ryx|B|2018-10-19|K|+3.1;
  3r16|A|2018-10-19|K|+3.1;
  3qyk|A|2018-10-19|S|+3.1;
  3p5l|A|2018-10-19|S|+3.1;
  4lhi|A|2018-10-19|S|+3.1;
  4kuy|A|2018-10-19|K|+3.1;
  4n16|A|2018-10-19|S|+3.1;
  4mlx|A|2018-10-19|S|+3.1;
  3sbh|A|2018-10-19|S|+3.1;
  3sap|A|2018-10-19|S|+3.1;
  3s9t|A|2018-10-19|S|+3.1;
  3s78|B|2018-10-19|S|+3.1;
  3s74|B|2018-10-19|K|+3.1;
  3s71|B|2018-10-19|S|+3.1;
  4kp8|A|2018-10-19|K|+3.1;
  4hu1|A|2018-10-19|S|+3.1;
  4r5a|A|2018-10-19|K|+3.1;
  4r5b|A|2018-10-19|S|+3.1;
  4cnr|A|2018-10-19|S|+3.1;
  4q6d|A|2018-10-19|S|+3.1;
  4qy3|A|2018-10-19|S|+3.1;
  4pyx|A|2018-10-19|K|+3.1;
  4qsi|A|2018-10-19|S|+3.1;
  5bnl|A|2018-10-19|S|+3.1;
  4q78|A|2018-10-19|S|+3.1;
  4qtl|A|2018-10-19|S|+3.1;
  4q8z|A|2018-10-19|K|+3.1;
  5fl6|A|2018-10-19|S|+3.1;
  4q90|A|2018-10-19|K|+3.1;
  4qjm|A|2018-10-19|K|+3.1;
  4rh2|A|2018-10-19|S|+3.1;
  4rux|A|2018-10-19|S|+3.1;
  4qjw|A|2018-10-19|S|+3.1;
  5amg|A|2018-10-19|S|+3.1;
  5a25|A|2018-10-19|S|+3.1;
  4q7w|A|2018-10-19|S|+3.1;
  4z1k|A|2018-10-19|K|+3.1;
  4q7v|A|2018-10-19|S|+3.1;
  5aml|A|2018-10-19|S|+3.1;
  4wl4|A|2018-10-19|K|+3.1;
  4zx1|A|2018-10-19|S|+3.1;
  4q81|A|2018-10-19|S|+3.1;
  4zao|A|2018-10-19|S|+3.1;
  5e2r|A|2018-10-19|S|+3.1;
  4pxx|A|2018-10-19|S|+3.1;
  4q8y|A|2018-10-19|S|+3.1;
  1a42|A|2018-10-18|S|+3.1;
  1bnv|A|2018-10-18|S|+3.1;
  1ca3|A|2018-10-18|S|+3.1;
  1caj|A|2018-10-18|S|+3.1;
  1cam|A|2018-10-18|S|+3.1;
  1cil|A|2018-10-18|S|+3.1;
  1cnc|A|2018-10-18|S|+3.1;
  1cnw|A|2018-10-18|S|+3.1;
  1cny|A|2018-10-18|S|+3.1;
  1crm|A|2018-10-18|S|+3.1;
  1cva|A|2018-10-18|S|+3.1;
  1cvc|A|2018-10-18|S|+3.1;
  1cvd|A|2018-10-18|S|+3.1;
  1flj|A|2018-10-18|S|+3.1;
  1fr7|A|2018-10-18|S|+3.1;
  1fsr|A|2018-10-18|K|+3.1;
  1hec|A|2018-10-18|S|+3.1;
  1i9l|A|2018-10-18|S|+3.1;
  1i9q|A|2018-10-18|S|+3.1;
  1kwr|A|2018-10-18|S|+3.1;
  1lg6|A|2018-10-18|S|+3.1;
  1lzv|A|2018-10-18|S|+3.1;
  1rze|A|2018-10-18|S|+3.1;
  1teu|X|2018-10-18|S|+3.1;
  1tg3|A|2018-10-18|S|+3.1;
  1tg9|A|2018-10-18|S|+3.1;
  1ugb|A|2018-10-18|S|+3.1;
  1urt|A|2018-10-18|K|+3.1;
  1xpz|A|2018-10-18|S|+3.1;
  1ydb|A|2018-10-18|S|+3.1;
  1yo1|A|2018-10-18|S|+3.1;
  1z93|A|2018-10-18|K|+3.1;
  2aw1|A|2018-10-18|S|+3.1;
  2hkk|A|2018-10-18|S|+3.1;
  2hl4|A|2018-10-18|S|+3.1;
  2ili|A|2018-10-18|K|+3.1;
  2nmx|A|2018-10-18|S|+3.1;
  2nn1|A|2018-10-18|S|+3.1;
  2nn7|A|2018-10-18|S|+3.1;
  2nwz|A|2018-10-18|K|+3.1;
  2nxr|A|2018-10-18|S|+3.1;
  2nxs|A|2018-10-18|S|+3.1;
  2osm|A|2018-10-18|S|+3.1;
  2pow|A|2018-10-18|K|+3.1;
  2q38|A|2018-10-18|S|+3.1;
  2wej|A|2018-10-18|K|+3.1;
  2weo|A|2018-10-18|S|+3.1;
  2x7t|A|2018-10-18|K|+3.1;
  3d9z|A|2018-10-18|S|+3.1;
  3dcc|A|2018-10-18|S|+3.1;
  3dvb|A|2018-10-18|K|+3.1;
  3dvc|A|2018-10-18|S|+3.1;
  3hfp|A|2018-10-18|S|+3.1;
  3hkt|A|2018-10-18|S|+3.1;
  3k2f|A|2018-10-18|S|+3.1;
  3k34|A|2018-10-18|K|+3.1;
  3kig|A|2018-10-18|S|+3.1;
  3kwa|A|2018-10-18|S|+3.1;
  3l14|A|2018-10-18|S|+3.1;
  3lxe|A|2018-10-18|S|+3.1;
  3m1w|A|2018-10-18|S|+3.1;
  3mnh|A|2018-10-18|S|+3.1;
  3rg3|A|2018-10-18|S|+3.1;
  3rg4|A|2018-10-18|S|+3.1;
  3rge|A|2018-10-18|S|+3.1;
  3rld|A|2018-10-18|S|+3.1;
  3tvn|X|2018-10-18|S|+3.1;
  3tvo|X|2018-10-18|S|+3.1;
  3u45|X|2018-10-18|S|+3.1;
  3u7c|A|2018-10-18|S|+3.1;
  3uyn|A|2018-10-18|K|+3.1;
  3uyq|A|2018-10-18|S|+3.1;
  3v3g|B|2018-10-18|S|+3.1;
  4cac|A|2018-10-18|S|+3.1;
  4m2v|A|2018-10-18|S|+3.1;
  3oim|A|2018-10-18|S|+3.1;
  3oil|A|2018-10-18|S|+3.1;
  3oku|A|2018-10-18|K|+3.1;
  3oy0|A|2018-10-18|S|+3.1;
  3m5s|A|2018-10-18|S|+3.1;
  3t83|A|2018-10-18|S|+3.1;
  3t84|A|2018-10-18|S|+3.1;
  3m2y|A|2018-10-18|S|+3.1;
  4jsw|A|2018-10-18|S|+3.1;
  4itp|A|2018-10-18|K|+3.1;
  4hf3|A|2018-10-18|S|+3.1;
  4hez|A|2018-10-18|S|+3.1;
  4hew|A|2018-10-18|K|+3.1;
  4fik|A|2018-10-18|K|+3.1;
  3oys|A|2018-10-18|K|+3.1;
  3p3h|A|2018-10-18|S|+3.1;
  3ml2|A|2018-10-18|K|+3.1;
  4e3g|A|2018-10-18|K|+3.1;
  4cq0|A|2018-10-18|S|+3.1;
  3rj7|A|2018-10-18|S|+3.1;
  3p5a|A|2018-10-18|K|+3.1;
  3p58|A|2018-10-18|S|+3.1;
  3p55|A|2018-10-18|K|+3.1;
  3p4v|A|2018-10-18|S|+3.1;
  4l5w|A|2018-10-18|S|+3.1;
  4k1q|A|2018-10-18|K|+3.1;
  3s77|B|2018-10-18|S|+3.1;
  4qef|A|2018-10-18|K|+3.1;
  4cnx|A|2018-10-18|S|+3.1;
  4riu|A|2018-10-18|S|+3.1;
  4q0l|A|2018-10-18|S|+3.1;
  4q06|A|2018-10-18|K|+3.1;
  4q7s|A|2018-10-18|S|+3.1;
  4rfd|A|2018-10-18|S|+3.1;
  4zx0|A|2018-10-18|S|+3.1;
  5amd|A|2018-10-18|K|+3.1;
  4zwi|A|2018-10-18|S|+3.1;
  4zwy|A|2018-10-18|S|+3.1;
  4zwx|A|2018-10-18|S|+3.1;
  5byi|A|2018-10-18|S|+3.1;
  4z1j|A|2018-10-18|K|+3.1;
  4y0j|A|2018-10-18|S|+3.1;
  5fl4|A|2018-10-18|S|+3.1;
  5brw|A|2018-10-18|K|+3.1;
  4q8x|A|2018-10-18|S|+3.1;
  1bnm|A|2018-10-17|S|+3.1;
  1ccu|A|2018-10-17|S|+3.1;
  1cim|A|2018-10-17|S|+3.1;
  1uge|A|2018-10-17|S|+3.1;
  1xeg|A|2018-10-17|S|+3.1;
  2geh|A|2018-10-17|S|+3.1;
  2h15|A|2018-10-17|S|+3.1;
  3da2|A|2018-10-17|S|+3.1;
  3n3j|A|2018-10-17|S|+3.1;
  3n4b|A|2018-10-17|S|+3.1;
  4knn|A|2018-10-17|K|+3.1;
  8ca2|A|2018-10-17|S|+3.1;
  4lp6|A|2018-10-17|S|+3.1;
  4ht0|A|2018-10-17|S|+3.1;
  4kuw|A|2018-10-17|S|+3.1;
  3sax|A|2018-10-17|K|+3.1;
  3s8x|A|2018-10-17|K|+3.1;
  3mdz|A|2018-10-17|S|+3.1;
  4knm|A|2018-10-17|S|+3.1;
  4q6e|A|2018-10-17|S|+3.1;
  4pzh|A|2018-10-17|S|+3.1;
  4qsa|A|2018-10-17|K|+3.1;
  4qiy|A|2018-10-17|S|+3.1;
  4qjx|A|2018-10-17|S|+3.1;
  4ruy|A|2018-10-17|S|+3.1;
  1h4n|A|2018-10-05|S|+3.1;
  2nwp|A|2018-10-05|S|+3.1;
  1g4j|A|2018-10-04|S|+3.1;
  3pjj|A|2018-10-04|S|+3.1;
  3s73|B|2018-10-04|K|+3.1;
  1avn|A|2018-10-03|S|+3.1;
  1ca2|A|2018-10-03|S|+3.1;
  1cnx|A|2018-10-03|S|+3.1;
  1g0e|A|2018-10-03|K|+3.1;
  1g1d|A|2018-10-03|S|+3.1;
  1g4o|A|2018-10-03|S|+3.1;
  1g52|A|2018-10-03|S|+3.1;
  1hca|A|2018-10-03|S|+3.1;
  1heb|A|2018-10-03|S|+3.1;
  1hed|A|2018-10-03|S|+3.1;
  1i8z|A|2018-10-03|S|+3.1;
  1i90|A|2018-10-03|S|+3.1;
  1i91|A|2018-10-03|S|+3.1;
  1i9m|A|2018-10-03|S|+3.1;
  1i9o|A|2018-10-03|S|+3.1;
  1i9p|A|2018-10-03|S|+3.1;
  1if5|A|2018-10-03|S|+3.1;
  1if7|A|2018-10-03|K|+3.1;
  1if8|A|2018-10-03|S|+3.1;
  1if9|A|2018-10-03|K|+3.1;
  1jd0|A|2018-10-03|S|+3.1;
  1kwq|A|2018-10-03|S|+3.1;
  1thk|A|2018-10-03|K|+3.1;
  1v9e|A|2018-10-03|S|+3.1;
  1ydc|A|2018-10-03|S|+3.1;
  2ca2|A|2018-10-03|S|+3.1;
  2cbb|A|2018-10-03|S|+3.1;
  2cbc|A|2018-10-03|K|+3.1;
  2ez7|A|2018-10-03|K|+3.1;
  2fmg|A|2018-10-03|S|+3.1;
  2fou|A|2018-10-03|S|+3.1;
  2nwy|A|2018-10-03|S|+3.1;
  2osf|A|2018-10-03|K|+3.1;
  4hba|A|2018-10-03|S|+3.1;
  4kap|A|2018-10-03|K|+3.1;
  4lu3|A|2018-10-03|K|+3.1;
  6ca2|A|2018-10-03|S|+3.1;
  4fvo|A|2018-10-03|S|+3.1;
  4fu5|A|2018-10-03|S|+3.1;
  4e49|A|2018-10-03|S|+3.1;
  3zp9|A|2018-10-03|S|+3.1;
  4l5u|A|2018-10-03|S|+3.1;
  4kv0|A|2018-10-03|S|+3.1;
  4kuv|A|2018-10-03|S|+3.1;
  4qjp|A|2018-10-03|S|+3.1;
  4q99|A|2018-10-03|S|+3.1;
  4rfc|A|2018-10-03|S|+3.1;
  4qjo|A|2018-10-03|S|+3.1;
  4q83|A|2018-10-03|S|+3.1;
  4q87|A|2018-10-03|S|+3.1;
  4q9y|A|2018-10-03|S|+3.1;
  2o4z|A|2018-10-02|S|+3.1;
  3b4f|A|2018-10-02|S|+3.1;
  3ca2|A|2018-10-02|S|+3.1;
  3f8e|A|2018-10-02|S|+3.1;
  3t85|A|2018-10-02|K|+3.1;
  3tmj|A|2018-10-02|S|+3.1;
  3rz0|B|2018-10-02|K|+3.1;
  1yda|A|2018-10-01|S|+3.1;
  2q1q|A|2018-10-01|S|+3.1;
  2weg|A|2018-10-01|S|+3.1;
  3bl0|A|2018-10-01|K|+3.1;
  3czv|A|2018-10-01|K|+3.1;
  3d0n|A|2018-10-01|S|+3.1;
  3dbu|A|2018-10-01|S|+3.1;
  3efi|A|2018-10-01|S|+3.1;
  3eft|A|2018-10-01|S|+3.1;
  3ffp|X|2018-10-01|S|+3.1;
  3kok|A|2018-10-01|S|+3.1;
  3okv|A|2018-10-01|K|+3.1;
  3v5g|A|2018-10-01|S|+3.1;
  3sbi|A|2018-10-01|K|+3.1;
  4cnw|A|2018-10-01|S|+3.1;
  1bcd|A|2018-09-29|S|+3.1;
  1bic|A|2018-09-29|S|+3.1;
  1can|A|2018-09-29|S|+3.1;
  1cin|A|2018-09-29|S|+3.1;
  1cra|A|2018-09-29|S|+3.1;
  1czm|A|2018-09-29|S|+3.1;
  1fqm|A|2018-09-29|K|+3.1;
  1jv0|A|2018-09-29|S|+3.1;
  1lg5|A|2018-09-29|S|+3.1;
  1rza|A|2018-09-29|S|+3.1;
  1rzc|A|2018-09-29|S|+3.1;
  1rzd|A|2018-09-29|S|+3.1;
  1ugf|A|2018-09-29|S|+3.1;
  2fos|A|2018-09-29|K|+3.1;
  9ca2|A|2018-09-29|S|+3.1;
  1kop|A|2018-09-29|S|+3.1;
  1lug|A|2018-09-28|S|+3.1;
  1tbt|X|2018-09-28|S|+3.1;
  1xev|A|2018-09-28|K|+3.1;
  1yo2|A|2018-09-28|S|+3.1;
  2hd6|A|2018-09-28|S|+3.1;
  2nxt|A|2018-09-28|K|+3.1;
  2wd2|A|2018-09-28|S|+3.1;
  2x7u|A|2018-09-28|S|+3.1;
  3d8w|A|2018-09-28|S|+3.1;
  3dd8|A|2018-09-28|S|+3.1;
  3pyk|A|2018-09-28|S|+3.1;
  3u47|A|2018-09-28|S|+3.1;
  4riv|A|2018-09-27|S|+3.1;
  1f2w|A|2018-09-26|S|+3.1;
  2abe|A|2018-09-26|S|+3.1;
  2ax2|A|2018-09-26|K|+3.1;
  1cng|A|2018-09-12|K|+3.1;
  1cnh|A|2018-09-12|K|+3.1;
  1cvf|A|2018-09-12|S|+3.1;
  1fqn|A|2018-09-12|S|+3.1;
  1fsn|A|2018-09-12|K|+3.1;
  1hva|A|2018-09-12|K|+3.1;
  1zsa|A|2018-09-12|K|+3.1;
  2cbe|A|2018-09-12|K|+3.1;
  2w2j|A|2018-09-12|K|+3.1;
  3bet|A|2018-09-12|K|+3.1;
  3c7p|A|2018-09-12|S|+3.1;
  3caj|A|2018-09-12|K|+3.1;
  3d93|A|2018-09-12|S|+3.1;
  3iai|A|2018-09-12|S|+3.1;
  3ibi|A|2018-09-12|S|+3.1;
  3ibl|A|2018-09-12|K|+3.1;
  3ibn|A|2018-09-12|K|+3.1;
  3ibu|A|2018-09-12|K|+3.1;
  3m2n|A|2018-09-12|K|+3.1;
  3m3x|A|2018-09-12|K|+3.1;
  3m40|A|2018-09-12|K|+3.1;
  3m5e|A|2018-09-12|K|+3.1;
  3m67|A|2018-09-12|K|+3.1;
  3m96|A|2018-09-12|K|+3.1;
  3m98|A|2018-09-12|K|+3.1;
  3mhi|A|2018-09-12|S|+3.1;
  3mhl|A|2018-09-12|K|+3.1;
  3mhm|A|2018-09-12|K|+3.1;
  3mho|A|2018-09-12|S|+3.1;
  3po6|A|2018-09-12|K|+3.1;
  3ryy|A|2018-09-12|S|+3.1;
  4bf6|A|2018-09-12|S|+3.1;
  3ryz|A|2018-09-12|S|+3.1;
  3s76|A|2018-09-12|K|+3.1;
  3rz8|A|2018-09-12|S|+3.1;
  3rz7|A|2018-09-12|K|+3.1;
  3rz5|A|2018-09-12|K|+3.1;
  4gge|A|2014-07-31|K|+3.1;
  1y7w|A|2014-07-31|K|+3.1;
  1znc|A|2014-07-31|K|+3.1;
  2znc|A|2014-07-31|K|+3.1;
  3b1b|A|2014-07-31|K|+3.1;
  3f7b|A|2014-07-31|K|+3.1;
  3f7u|A|2014-07-31|S|+3.1;
  3fw3|A|2014-07-31|K|+3.1;
  3znc|A|2014-07-31|K|+3.1;

Knot types		pdb	Title
S +3₁		3m1wA	Carbonic anhyrdase ii mutant w5ch64c with closed disulfide bond in complex with sulfate
S +3₁		3mnhA	Human carbonic anhydrase ii mutant k170a
S +3₁		3rg3A	Crystal structure of the w5e mutant of human carbonic anhydrase ii
S +3₁		3rg4A	Crystal structure of the w5f mutant of human carbonic anhydrase ii
S +3₁		3rgeA	Crystal structure of the w5h mutant of human carbonic anhydrase ii
S +3₁		3rldA	Crystal structure of the y7i mutant of human carbonic anhydrase ii
S +3₁		3tvnX	Human carbonic anhydrase ii proton transfer mutant
S +3₁		3tvoX	Human carbonic anhydrase ii proton transfer double mutant
S +3₁		3u45X	Human carbonic anhydrase ii v143a
S +3₁		3u7cA	Crystal structure of the v143i mutant of human carbonic anhydrase ii
K +3₁		3uynA	Hca 3
S +3₁		3uyqA	Hca 3
S +3₁		3v3gB	Kinetic and structural studies of thermostabilized mutants of hca ii.
S +3₁		4cacA	Refined structure of human carbonic anhydrase ii at 2.0 angstroms resolution
S +3₁		4m2vA	Genetically engineered carbonic anhydrase ix in complex with brinzolamide
S +3₁		3oimA	Human carbonic anhydrase ii bound by 2-ethylestradiol 3-o-sulfamate
S +3₁		3oilA	Human carbonic anhydrase ii mutant a65s, n67q (ca ix mimic) bound by 2-ethylestradiol 3-o-sulfamate
K +3₁		3okuA	Human carbonic anhydrase ii in complex with 2-ethylestrone-3-o-sulfamate
S +3₁		3oy0A	Human carbonic anhydrase ii complexed with 1-(4-(4-(2-(isopropylsulfonyl)phenylamino)-1h-pyrrolo[2,3-b]pyridin-6-ylamino)-3-methoxyphenyl)piperidin-4-ol
S +3₁		3m5sA	Carbonic anhydrase ii mutant h64c in complex with carbonate
S +3₁		3t83A	Human carbonic anhydrase ii in complex with acetylated carbohydrate sulfamates
S +3₁		3t84A	Human carbonic anhydrase ii in complex with acetylated carbohydrate sulfamates
S +3₁		3m2yA	Carbonic anhydrase ii in complex with novel sulfonamide inhibitor
S +3₁		4jswA	Human carbonic anhydrase ii h94c
K +3₁		4itpA	Structure of human carbonic anhydrase ii bound to a benzene sulfonamide
S +3₁		4hf3A	Activity enhancers of h64a variant of human carbonic anhydrase ii possess multiple binding sites within and around the enzyme structure
S +3₁		4hezA	Activity enhancers of h64a variant of human carbonic anhydrase ii possess multiple binding sites within and around the enzyme structure
K +3₁		4hewA	Activity enhancers of h64a variant of human carbonic anhydrase ii possess multiple binding sites within and around the enzyme structure
K +3₁		4fikA	Human carbonic anhydrase ii h64a complexed with thioxolone hydrolysis products
K +3₁		3oysA	Human carbonic anhydrase ii complexed with 2-{[4-amino-3-(3-hydroxyprop-1-yn-1-yl)-1h-pyrazolo[3,4-d]pyrimidin-1-yl]methyl}-5-methyl-3-(2-methylphenyl)quinazolin-4(3h)-one
S +3₁		3p3hA	Human carbonic anhydrase ii in complex with p-(5-ferrocenyl-1h-1,2,3-triazol-1-yl)benzenesulfonamide
K +3₁		3ml2A	Human carbonic anhydsase ii in complex with an aryl sulfonamide inhibitor
K +3₁		4e3gA	Nucleophile recognition as an alternative inhibition mode for benzoic acid based carbonic anhydrase inhibitors
S +3₁		4cq0A	Cyclic secondary sulfonamides: unusually good inhibitors of cancer- related carbonic anhydrase enzymes
S +3₁		3rj7A	Human carbonic anhydrase ii complexed with its inhibitor rhenium(i)triscarbonyl-cyclopentadienyl-carboxy-4-aminomethylbenzene-sulfonamide
K +3₁		3p5aA	Human carbonic anhydrase complexed with sodium morpholinocarbodithioate
S +3₁		3p58A	Human carbonic anhydrase in complex with benzyl (methyl) carbamodithoic acid
K +3₁		3p55A	Human carbonic anhydrase ii in complex with p-(4-ferrocenyl-1h-1,2,3-triazol-1-yl)benzenesulfonamide
S +3₁		3p4vA	Human carbonic anhydrase ii in complex with (+)-xylariamide a
S +3₁		4l5wA	Structural implications of the secondary co2 binding pocket in human carbonic anhydrase ii
K +3₁		4k1qA	Structure of hcaix mimic (hcaii with 5 mutations in active site)
S +3₁		3s77B	The origin of the hydrophobic effect in the molecular recognition of arylsulfonamides by carbonic anhydrase
K +3₁		4qefA	Human carbonic anhydrase ii v207i - cyanate inhibitor complex
S +3₁		4cnxA	Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion co2 capture
S +3₁		4riuA	A carbonic anhydrase ix mimic in complex with a saccharin-based inhibitor
S +3₁		4q0lA	Crystal structure of catalytic domain of human carbonic anhydrase isozyme xii with inhibitor
K +3₁		4q06A	Crystal structure of chimeric carbonic anhydrase ix with inhibitor
S +3₁		4q7sA	Crystal structure of 1-hydroxy-4-methylpyridine-2(1h)-thione bound to human carbonic anhydrase ii
S +3₁		4rfdA	Human carbonic anhydrase ii in complex with 4-(4-sulfamoyl-phenoxy)-butylammonium
S +3₁		4zx0A	Human carbonic anhydrase ii in complex with a glucosyl sulfamate inhibitor
K +3₁		5amdA	Three dimensional structure of human carbonic anhydrase ii in complex with 2-((2-phenylethyl)sulfamoyl)-4-sulfamoylbenzoic acid
S +3₁	₄	4zwiA	Surface lysine acetylated human carbonic anhydrase ii in complex with a sulfamate-based inhibitor
S +3₁		4zwyA	Human carbonic anhydrase ii in complex with a glucosyl sulfamate inhibitor
S +3₁		4zwxA	Engineered carbonic anhydrase ix mimic in complex with glucosyl sulfamate inhibitor
S +3₁		5byiA	Human carbonic anhydrase ii with an azobenzene inhibitor (1d)
K +3₁		4z1jA	Carbonic anhydrase inhibitors: design and synthesis of new heteroaryl-n-carbonylbenzenesulfonamides targeting druggable human carbonic anhydrase isoforms (hca vii, hca ix, and hca xiv)
S +3₁		4y0jA	H/d exchanged human carbonic anhydrase ii ph 6 room temperature neutron crystal structure.
S +3₁		5fl4A	Three dimensional structure of human carbonic anhydrase ix in complex with 5-(1-naphthalen-1-yl-1,2,3-triazol-4-yl)thiophene-2-sulfonamide
K +3₁		5brwA	Catalytic improvement of an artificial metalloenzyme by computational design
S +3₁		4q8xA	Crystal structure of 1-hydroxy-5-(trifluoromethyl)pyridine-2(1h)-thione bound to human carbonic anhydrase ii
S +3₁		1bnmA	Carbonic anhydrase ii inhibitor
S +3₁		1ccuA	Structure-assisted redesign of a protein-zinc binding site with femtomolar affinity
S +3₁		1cimA	The positions of his-64 and a bound water in human carbonic anhydrase ii upon binding three structurally related inhibitors
S +3₁		1ugeA	Human carbonic anhydrase ii [hcaii] (e.c.4.2.1.1) mutant with ala 65 replaced by leu (a65l)
S +3₁		1xegA	Crystal structure of human carbonic anhydrase ii complexed with an acetate ion
S +3₁		2gehA	N-hydroxyurea, a versatile zinc binding function in the design of metalloenzyme inhibitors
S +3₁		2h15A	Carbonic anhydrase inhibitors: clashing with ala65 as a means of designing isozyme-selective inhibitors that show low affinity for the ubiquitous isozyme ii
S +3₁		3da2A	X-ray structure of human carbonic anhydrase 13 in complex with inhibitor
S +3₁		3n3jA	Crystal structure of human carbonic anhydrase ii in complex with a benzenesulfonamide inhibitor
S +3₁		3n4bA	Crystal structure of human carbonic anhydrase ii in complex with a benzenesulfonamide inhibitor
K +3₁		4knnA	Crystal structure of human carbonic anhydrase isozyme xiii with 2-chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide
S +3₁		8ca2A	Engineering the hydrophobic pocket of carbonic anhydrase ii
S +3₁		4lp6A	Crystal structure of human carbonic anhydrase ii in complex with a quinoline oligoamide foldamer
S +3₁		4ht0A	Crystal structure of human carbonic anhydrase isozyme ii with the inhibitor.
S +3₁		4kuwA	Crystal structure of human carbonic anhydrase ii in complex with the 5-(3-(4-fluorophenylsulfonyl)ureido)pyridine-2-sulfonamide inhibitor
K +3₁		3saxA	Crystal structure of human carbonic anhydrase isozyme ii with 2-chloro-5-{[(5-ethyl-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide
K +3₁		3s8xA	Crystal structure of human carbonic anhydrase isozyme ii with 4-{[(4-methyl-6-oxo-1,6-dihydro-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide
S +3₁		3mdzA	Crystal structure of human carbonic anhydrase vii [isoform 1], ca7
S +3₁		4knmA	Crystal structure of human carbonic anhydrase isozyme xiii with 2-chloro-4-{[(4,6-dimethylpyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide
S +3₁		4q6eA	Crystal structure of human carbonic anhydrase isozyme ii with 4-{[3-(3,5-dimethyl-1h-pyrazol-1-yl)-3-oxopropyl]amino}benzene-1-sulfonamide
S +3₁		4pzhA	Crystal structure of human carbonic anhydrase isozyme ii with 2,3,5,6-tetrafluoro-4[(2-hydroxyethyl)sulfonyl]benzenesulfonamide
K +3₁		4qsaA	Crystal structure of human carbonic anhydrase isozyme ii with 2-chloro-4-{[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)thio]acetyl}benzenesulfonamide
S +3₁		4qiyA	Crystal structure of human carbonic anhydrase isozyme ii with inhibitor
S +3₁		4qjxA	Crystal structure of human carbonic anhydrase isozyme xiii with inhibitor
S +3₁		4ruyA	Crystal structure of human carbonic anhydrase ii in complex with 4-propoxybenzenesulfonamide
S +3₁		1h4nA	H94n carbonic anhydrase ii complexed with tris
S +3₁		2nwpA	Structural and kinetic effects of hydrophobic mutations in the active site of human carbonic anhydrase ii
S +3₁		1g4jA	Carbonic anhydrase ii (f131v) complexed with 4-(aminosulfonyl)-n-[(2,3,4,5,6-pentafluorophenyl)methyl]-benzamide
S +3₁		3pjjA	Synthetic dimer of human carbonic anhydrase ii
K +3₁		3s73B	The origin of the hydrophobic effect in the molecular recognition of arylsulfonamides by carbonic anhydrase
S +3₁		1avnA	Human carbonic anhydrase ii complexed with the histamine activator
S +3₁		1ca2A	Refined structure of human carbonic anhydrase ii at 2.0 angstroms resolution
S +3₁		1cnxA	Secondary interactions significantly removed from the sulfonamide binding pocket of carbonic anhydrase ii influence binding constants
K +3₁		1g0eA	Site-specific mutant (his64 replaced with ala) of human carbonic anhydrase ii complexed with 4-methylimidazole
S +3₁		1g1dA	Carbonic anhydrase ii complexed with 4-(aminosulfonyl)-n-[(2-fluorophenyl)methyl]-benzamide
S +3₁		1g4oA	Carbonic anhydrase ii (f131v) complexed with 4-(aminosulfonyl)-n-phenylmethylbenzamide
S +3₁		1g52A	Carbonic anhydrase ii complexed with 4-(aminosulfonyl)-n-[(2,3-difluorophenyl)methyl]-benzamide
S +3₁		1hcaA	Unexpected ph-dependent conformation of his-64, the proton shuttle of carbonic anhydrase ii.
S +3₁		1hebA	Structural consequences of hydrophilic amino-acid substitutions in the hydrophobic pocket of human carbonic anhydrase ii
S +3₁		1hedA	Structural consequences of hydrophilic amino-acid substitutions in the hydrophobic pocket of human carbonic anhydrase ii
S +3₁		1i8zA	Carbonic anhydrase ii complexed with al-6629 2h-thieno[3,2-e]-1,2-thiazine-6-sulfonamide, 2-(3-methoxyphenyl)-3-(4-morpholinyl)-, 1,1-dioxide
S +3₁		1i90A	Carbonic anhydrase ii complexed with al-8520 2h-thieno[3,2-e]-1,2-thiazine-6-sulfonamide, 4-amino-3,4-dihydro-2-(3-methoxypropyl)-, 1,1-dioxide, (r)
S +3₁		1i91A	Carbonic anhydrase ii complexed with al-6619 2h-thieno[3,2-e]-1,2-thiazine-6-sulfonamide, 2-(3-hydroxyphenyl)-3-(4-morpholinyl)-, 1,1-dioxide
S +3₁		1i9mA	Carbonic anhydrase ii (f131v) complexed with 4-(aminosulfonyl)-n-[(2,4-difluorophenyl)methyl]-benzamide
S +3₁		1i9oA	Carbonic anhydrase ii (f131v) complexed with 4-(aminosulfonyl)-n-[(2,3,4-trifluorophenyl)methyl]-benzamide
S +3₁		1i9pA	Carbonic anhydrase ii (f131v) complexed with 4-(aminosulfonyl)-n-[(2,4,6-trifluorophenyl)methyl]-benzamide
S +3₁		1if5A	Carbonic anhydrase ii complexed with 2,6-difluorobenzenesulfonamide
K +3₁		1if7A	Carbonic anhydrase ii complexed with (r)-n-(3-indol-1-yl-2-methyl-propyl)-4-sulfamoyl-benzamide
S +3₁		1if8A	Carbonic anhydrase ii complexed with (s)-n-(3-indol-1-yl-2-methyl-propyl)-4-sulfamoyl-benzamide
K +3₁		1if9A	Carbonic anhydrase ii complexed with n-[2-(1h-indol-5-yl)-butyl]-4-sulfamoyl-benzamide
S +3₁		1jd0A	Crystal structure of the extracellular domain of human carbonic anhydrase xii complexed with acetazolamide
S +3₁		1kwqA	Human carbonic anhydrase ii complexed with inhibitor 2000-07
K +3₁		1thkA	Effect of shuttle location and ph environment on h+ transfer in human carbonic anhydrase ii
S +3₁		1v9eA	Crystal structure analysis of bovine carbonic anhydrase ii
S +3₁		1ydcA	Structural basis of inhibitor affinity to variants of human carbonic anhydrase ii
S +3₁		2ca2A	Crystallographic studies of inhibitor binding sites in human carbonic anhydrase ii. a pentacoordinated binding of the scn-ion to the zinc at high p*h
S +3₁		2cbbA	Structure of native and apo carbonic anhydrase ii and some of its anion-ligand complexes
K +3₁		2cbcA	Structure of native and apo carbonic anhydrase ii and some of its anion-ligand complexes
K +3₁		2ez7A	Carbonic anhydrase activators. activation of isozymes i, ii, iv, va, vii and xiv with l- and d-histidine and crystallographic analysis of their adducts with isoform ii: engineering proton transfer processes within the active site of an enzyme
S +3₁		2fmgA	Carbonic anhydrase activators. activation of isoforms i, ii, iv, va, vii and xiv with l- and d- phenylalanine and crystallographic analysis of their adducts with isozyme ii: sterospecific recognition within the active site of an enzyme and its consequences for the drug design, structure with l-phenylalanine
S +3₁	₄	2fouA	Human carbonic anhydrase ii complexed with two-prong inhibitors
S +3₁		2nwyA	Structural and kinetic effects of hydrophobic mutations on the active site of human carbonic anhydrase ii
K +3₁		2osfA	Inhibition of carbonic anhydrase ii by thioxolone: a mechanistic and structural study
S +3₁		4hbaA	Structural and catalytic characterization of a thermal and acid stable variant of human carbonic anhydrase ii containing an engineered disulfide bond
K +3₁		4kapA	The binding of benzoarylsulfonamide ligands to human carbonic anhydrase is insensitive to formal fluorination of the ligand
K +3₁		4lu3A	The crystal structure of the human carbonic anhydrase xiv
S +3₁		6ca2A	Engineering the hydrophobic pocket of carbonic anhydrase ii
S +3₁		4fvoA	Carbonic anhydrase ii in complex with n-[(2e)-3,4-dihydroquinazolin-2(1h)-ylidene]sulfuric diamide
S +3₁		4fu5A	Carbonic anhydrase ii in complex with n-[(2z)-1,3-oxazolidin-2-ylidene]sulfuric diamide
S +3₁		4e49A	Nucleophile recognition as an alternative inhibition mode for benzoic acid based carbonic anhydrase inhibitors
S +3₁		3zp9A	Human carbonic anhydrase ii as a scaffold for an artificial transfer hydrogenase
S +3₁		4l5uA	The structural implications of the secondary co2 binding pocket in human carbonic anhydrase ii
S +3₁		4kv0A	Crystal structure of human carbonic anhydrase ii in complex with the 5-(3-tosylureido)pyridine-2-sulfonamide inhibitor
S +3₁		4kuvA	Crystal structure of human carbonic anhydrase ii in complex with the 5-(3-(4-chlorophenylsulfonyl)ureido)pyridine-2-sulfonamide inhibitor
S +3₁		4qjpA	Crystal structure of human carbonic anhydrase isozyme xiii with inhibitor
S +3₁		4q99A	Crystal structure of 2-mercapto-4-methylphenol bound to human carbonic anhydrase ii
S +3₁		4rfcA	Human carbonic anhydrase ii in complex with tert-butyl 4-(4-sulfamoylphenoxy)butylcarbamate
S +3₁		4qjoA	Crystal structure of catalytic domain of human carbonic anhydrase isozyme xii with inhibitor
S +3₁		4q83A	Crystal structure of 1-hydroxy-3-(trifluoromethyl)pyridine-2(1h)-thione bound to human carbonic anhydrase ii
S +3₁		4q87A	Crystal structure of 1-hydroxy-4-(trifluoromethyl)pyridine-2(1h)-thione bound to human carbonic anhydrase ii
S +3₁		4q9yA	Crystal structure of 3-methylthiophenol bound to human carbonic anhydrase ii
S +3₁		2o4zA	Crystal structure of the carbonic anhydrase ii complexed with hydroxysulfamide inhibitor
S +3₁		3b4fA	Carbonic anhydrase inhibitors. interaction of 2-(hydrazinocarbonyl)-3-phenyl-1h-indole-5-sulfonamide with twelve mammalian isoforms: kinetic and x-ray crystallographic studies
S +3₁		3ca2A	Crystallographic studies of inhibitor binding sites in human carbonic anhydrase ii. a pentacoordinated binding of the scn-ion to the zinc at high p*h
S +3₁		3f8eA	Coumarins are a novel class of suicide carbonic anhydrase inhibitors
K +3₁		3t85A	Human carbonic anhydrase ii in complex with acetylated carbohydrate sulfamates
S +3₁		3tmjA	Joint x-ray/neutron structure of human carbonic anhydrase ii at ph 7.8
K +3₁		3rz0B	Fluoroalkyl and alkyl chains have similar hydrophobicities in binding to the hydrophobic wall of carbonic anhydrase
S +3₁		1ydaA	Structural basis of inhibitor affinity to variants of human carbonic anhydrase ii
S +3₁		2q1qA	Carbonic anhydrase inhibitors. interaction of the antiepileptic drug sulthiame with twelve mammalian isoforms: kinetic and x-ray crystallographic studies

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