Found 363 chains in Knotted chains table. Displaying 151 - 300. Applied filters: Probabilistic

Search results query: Carbonic Anhydrase II

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#pdbid|chain|deposition date|is S/K-not|(slip)knot types;
      
  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;
  3iqk|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;
  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;
  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;
  3mna|A|2018-10-20|S|+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;
  3nj9|A|2018-10-20|S|+3.1;
  3oik|A|2018-10-20|S|+3.1;
  4ca2|A|2018-10-20|S|+3.1;
  7ca2|A|2018-10-20|S|+3.1;
  3r17|B|2018-10-20|S|+3.1;
  1te3|X|2018-10-20|S|+3.1;
  2vvb|X|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;
  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;
  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;
  3m1q|A|2018-10-19|K|+3.1;
  3m2z|A|2018-10-19|S|+3.1;
  3m5t|A|2018-10-19|S|+3.1;
  3mmf|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;
  3ni5|A|2018-10-19|S|+3.1;
  3r16|A|2018-10-19|K|+3.1;
  5ca2|A|2018-10-19|S|+3.1;
  5cac|A|2018-10-19|S|+3.1;
  1v9i|C|2018-10-19|S|+3.1;
  2vva|X|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;
  1tg3|A|2018-10-18|S|+3.1;
  1tg9|A|2018-10-18|S|+3.1;
  1ugb|A|2018-10-18|S|+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;
  2hfx|A|2018-10-18|K|+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;
  3m2y|A|2018-10-18|S|+3.1;
  3m5s|A|2018-10-18|S|+3.1;
  3ml2|A|2018-10-18|K|+3.1;
  3mnh|A|2018-10-18|S|+3.1;
  3oil|A|2018-10-18|S|+3.1;
  3oim|A|2018-10-18|S|+3.1;
  3oku|A|2018-10-18|K|+3.1;
  3p4v|A|2018-10-18|S|+3.1;
  4cac|A|2018-10-18|S|+3.1;
  1teu|X|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;
  3mdz|A|2018-10-17|S|+3.1;
  3n3j|A|2018-10-17|S|+3.1;
  3n4b|A|2018-10-17|S|+3.1;
  8ca2|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;
  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;
  6ca2|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;
  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;
  3kok|A|2018-10-01|S|+3.1;
  3okv|A|2018-10-01|K|+3.1;
  3ffp|X|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;
  1kop|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;
  1lug|A|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;
  1tbt|X|2018-09-28|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;
  1y7w|A|2014-07-31|K|+3.1;
  1znc|A|2014-07-31|K|+3.1;
  2hfy|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;
  3jxf|A|2014-07-31|K|+3.1;
  3jxg|A|2014-07-31|K|+3.1;
  3znc|A|2014-07-31|K|+3.1;
  3jxh|C|2014-07-31|K|+3.1;

      
Knot types Knot loop types pdb Title
S +31 S 3x +31 3ni5A Carbonic anhydrase inhibitor: c1 family
K +31 K 3x +31 3r16A Human caii bound to n-(4-sulfamoylphenyl)-2-(thiophen-2-yl) acetamide
S +31 S 22x +31 5ca2A Conformational mobility of his-64 in the thr-200 (right arrow) ser mutant of human carbonic anhydrase ii
S +31 S 3x +31 5cacA Refined structure of human carbonic anhydrase ii at 2.0 angstroms resolution
S +31 S 3x +31 1v9iC Crystal structure analysis of the site specific mutant (q253c) of bovine carbonic anhydrase ii
S +31 S 3x +31 2vvaX Human carbonic anhydrase in complex with co2
S +31 S 11x +31 1a42A Human carbonic anhydrase ii complexed with brinzolamide
S +31 S 23x +31 1bnvA Carbonic anhydrase ii inhibitor
S +31 S 7x +31 1ca3A Unexpected ph-dependent conformation of his-64, the proton shuttle of carbonic anhydrase ii.
S +31 S 3x +31 1cajA Structural analysis of the zinc hydroxide-thr 199-glu 106 hydrogen bonding network in human carbonic anhydrase ii
S +31 S 3x +31 1camA Structural analysis of the zinc hydroxide-thr 199-glu 106 hydrogen bonding network in human carbonic anhydrase ii
S +31 S 2x +31 1cilA The positions of his-64 and a bound water in human carbonic anhydrase ii upon binding three structurally related inhibitors
S +31 S 3x +31 1cncA Compensatory plastic effects in the redesign of protein-zinc binding sites
S +31 S 11x +31 1cnwA Secondary interactions significantly removed from the sulfonamide binding pocket of carbonic anhydrase ii influence binding constants
S +31 S 11x +31 1cnyA Secondary interactions significantly removed from the sulfonamide binding pocket of carbonic anhydrase ii influence binding constants
S +31 S 3x +31 1crmA Structure and function of carbonic anhydrases
S +31 S 3x +31 1cvaA Structural and functional importance of a conserved hydrogen bond network in human carbonic anhydrase ii
S +31 S 3x +31 1cvcA Redesigning the zinc binding site of human carbonic anhydrase ii: structure of a his2asp-zn2+ metal coordination polyhedron
S +31 S 3x +31 1cvdA Structural consequences of redesigning a protein-zinc binding site
S +31 S 3x +31 1fljA Crystal structure of s-glutathiolated carbonic anhydrase iii
S +31 S 3x +31 1fr7A X-ray crystal structure of zinc-bound f93s/f95l/w97m carbonic anhydrase (caii) variant
K +31 K 3x +31 1fsrA X-ray crystal structure of copper-bound f93s/f95l/w97m carbonic anhydrase (caii) variant
S +31 S 3x +31 1hecA Structural consequences of hydrophilic amino-acid substitutions in the hydrophobic pocket of human carbonic anhydrase ii
S +31 S 15x +31 1i9lA Carbonic anhydrase ii (f131v) complexed with 4-(aminosulfonyl)-n-[(4-fluorophenyl)methyl]-benzamide
S +31 S 7x +31 1i9qA Carbonic anhydrase ii (f131v) complexed with 4-(aminosulfonyl)-n-[(3,4,5-trifluorophenyl)methyl]-benzamide
S +31 S 3x +31 1kwrA Human carbonic anhydrase ii complexed with inhibitor 0134-36
S +31 S 3x +31 1lg6A Crystal structure analysis of hca ii mutant t199p in complex with thiocyanate
S +31 S 3x +31 1lzvA Site-specific mutant (tyr7 replaced with his) of human carbonic anhydrase ii
S +31 S 3x +31 1rzeA X-ray analysis of metal substituted human carbonic anhydrase ii derivatives
S +31 S 3x +31 1tg3A Effect of shuttle location and ph environment on h+ transfer in human carbonic anhydrase ii
S +31 S 3x +31 1tg9A Effect of shuttle location and ph environment on h+ transfer in human carbonic anhydrase ii
S +31 S 3x +31 1ugbA Human carbonic anhydrase ii[hcaii] (e.c.4.2.1.1) mutant with ala 65 replaced by gly (a65g)
S +31 S 3x +31 1xpzA Structure of human carbonic anhydrase ii with 4-[4-o-sulfamoylbenzyl)(4-cyanophenyl)amino]-4h-[1,2,4]-triazole
S +31 S 23x +31 1ydbA Structural basis of inhibitor affinity to variants of human carbonic anhydrase ii
S +31 S 3x +31 1yo1A Proton transfer from his200 in human carbonic anhydrase ii
K +31 K 3x +31 1z93A Human carbonic anhydrase iii:structural and kinetic study of catalysis and proton transfer.
S +31 S 3x +31 2aw1A Carbonic anhydrase inhibitors: valdecoxib binds to a different active site region of the human isoform ii as compared to the structurally related cyclooxygenase ii "selective" inhibitor celecoxib
K +31 K 1x +31 2hfxA Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase iii
S +31 S 11x +31 2hkkA Carbonic anhydrase activators: solution and x-ray crystallography for the interaction of andrenaline with various carbonic anhydrase isoforms
S +31 S 11x +31 2hl4A Crystal structure analysis of human carbonic anhydrase ii in complex with a benzenesulfonamide derivative
K +31 K 3x +31 2iliA Refine atomic structure of human carbonic anhydrase ii
S +31 S 3x +31 2nmxA Structure of inhibitor binding to carbonic anhydrase i
S +31 S 3x +31 2nn1A Structure of inhibitor binding to carbonic anhydrase i
S +31 S 3x +31 2nn7A Structure of inhibitor binding to carbonic anhydrase i
K +31 K 3x +31 2nwzA Structural and kinetic effects of hydrophobic mutations on the active site of human carbonic anhydrase ii
S +31 S 3x +31 2nxrA Structural effects of hydrophobic mutations on the active site of human carbonic anhydrase ii
S +31 S 3x +31 2nxsA Structural and kinetic effects of hydrophobic mutations in the active site of human carbonic anhydrase ii
S +31 S 3x +31 2osmA Inhibition of carbonic anhydrase ii by thioxolone: a mechanistic and structural study
K +31 K 3x +31 2powA The crystal structure of the human carbonic anhydrase ii in complex with 4-amino-6-trifluoromethyl-benzene-1,3-disulfonamide
S +31 S 3x +31 2q38A Carbonic anhydrase ii in complex with saccharin at 1.95 angstrom
K +31 K 3x +31 2wejA Thermodynamic optimisation of carbonic anhydrase fragment inhibitors
S +31 S 3x +31 2weoA Thermodynamic optimisation of carbonic anhydrase fragment inhibitors
K +31 K 2x +31 2x7tA Structures of human carbonic anhydrase ii inhibitor complexes reveal a second binding site for steroidal and non-steroidal inhibitors.
S +31 S 3x +31 3d9zA Use of carbonic anhydrase ii, ix active-site mimic, for the purpose of screening inhibitors for possible anti-cancer properties
S +31 S 3x +31 3dccA Use of carbonic anhydrase ii, ix active-site mimic, for the purpose of screening inhibitors for possible anti-cancer properties
K +31 K 3x +31 3dvbA X-ray crystal structure of mutant n62v human carbonic anhydrase ii
S +31 S 3x +31 3dvcA X-ray crystal structure of mutant n62t of human carbonic anhydrase ii
S +31 S 3x +31 3hfpA Crystal structure of teh complex between ca ii and the activator mai
S +31 S 3x +31 3hktA Human carbonic anhydrase ii in complex with alpha-d-glucopyranosyl-(1->4)-1-thio-beta-d-glucopyranosylsulfonamide
S +31 S 3x +31 3k2fA Nitric oxide-donating carbonic anhydrase inhibitors for the treatment of open-angle glaucoma
K +31 K 11x +31 3k34A Human carbonic anhydrase ii with a sulfonamide inhibitor
S +31 S 3x +31 3kigA Mutant carbonic anhydrase ii in complex with an azide and an alkyne
S +31 S 15x +31 3kwaA Polyamines inhibit carbonic anhydrases
S +31 S 3x +31 3l14A Human carbonic anhydrase ii complexed with althiazide
S +31 S 3x +31 3lxeA Human carbonic anhydrase i in complex with topiramate
S +31 S 3x +31 3m1wA Carbonic anhyrdase ii mutant w5ch64c with closed disulfide bond in complex with sulfate
S +31 S 7x +31 3m2yA Carbonic anhydrase ii in complex with novel sulfonamide inhibitor
S +31 S 3x +31 3m5sA Carbonic anhydrase ii mutant h64c in complex with carbonate
K +31 K 3x +31 3ml2A Human carbonic anhydsase ii in complex with an aryl sulfonamide inhibitor
S +31 S 3x +31 3mnhA Human carbonic anhydrase ii mutant k170a
S +31 S 3x +31 3oilA Human carbonic anhydrase ii mutant a65s, n67q (ca ix mimic) bound by 2-ethylestradiol 3-o-sulfamate
S +31 S 3x +31 3oimA Human carbonic anhydrase ii bound by 2-ethylestradiol 3-o-sulfamate
K +31 K 3x +31 3okuA Human carbonic anhydrase ii in complex with 2-ethylestrone-3-o-sulfamate
S +31 S 3x +31 3p4vA Human carbonic anhydrase ii in complex with (+)-xylariamide a
S +31 S 3x +31 4cacA Refined structure of human carbonic anhydrase ii at 2.0 angstroms resolution
S +31 S 3x +31 1teuX Effect of shuttle location and ph environment on h+ transfer in human carbonic anhydrase ii
S +31 S 11x +31 1bnmA Carbonic anhydrase ii inhibitor
S +31 S 3x +31 1ccuA Structure-assisted redesign of a protein-zinc binding site with femtomolar affinity
S +31 S 23x +31 1cimA The positions of his-64 and a bound water in human carbonic anhydrase ii upon binding three structurally related inhibitors
S +31 S 7x +31 1ugeA Human carbonic anhydrase ii [hcaii] (e.c.4.2.1.1) mutant with ala 65 replaced by leu (a65l)
S +31 S 3x +31 1xegA Crystal structure of human carbonic anhydrase ii complexed with an acetate ion
S +31 S 23x +31 2gehA N-hydroxyurea, a versatile zinc binding function in the design of metalloenzyme inhibitors
S +31 S 11x +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 S 1x +31 3da2A X-ray structure of human carbonic anhydrase 13 in complex with inhibitor
S +31 S 3x +31 3mdzA Crystal structure of human carbonic anhydrase vii [isoform 1], ca7
S +31 S 3x +31 3n3jA Crystal structure of human carbonic anhydrase ii in complex with a benzenesulfonamide inhibitor
S +31 S 3x +31 3n4bA Crystal structure of human carbonic anhydrase ii in complex with a benzenesulfonamide inhibitor
S +31 S 11x +31 8ca2A Engineering the hydrophobic pocket of carbonic anhydrase ii
S +31 S 3x +31 1h4nA H94n carbonic anhydrase ii complexed with tris
S +31 S 3x +31 2nwpA Structural and kinetic effects of hydrophobic mutations in the active site of human carbonic anhydrase ii
S +31 S 7x +31 1g4jA Carbonic anhydrase ii (f131v) complexed with 4-(aminosulfonyl)-n-[(2,3,4,5,6-pentafluorophenyl)methyl]-benzamide
S +31 S 11x +31 1avnA Human carbonic anhydrase ii complexed with the histamine activator
S +31 S 3x +31 1ca2A Refined structure of human carbonic anhydrase ii at 2.0 angstroms resolution
S +31 S 22x +31 1cnxA Secondary interactions significantly removed from the sulfonamide binding pocket of carbonic anhydrase ii influence binding constants
K +31 K 23x +31 1g0eA Site-specific mutant (his64 replaced with ala) of human carbonic anhydrase ii complexed with 4-methylimidazole
S +31 S 23x +31 1g1dA Carbonic anhydrase ii complexed with 4-(aminosulfonyl)-n-[(2-fluorophenyl)methyl]-benzamide
S +31 S 15x +31 1g4oA Carbonic anhydrase ii (f131v) complexed with 4-(aminosulfonyl)-n-phenylmethylbenzamide
S +31 S 7x +31 1g52A Carbonic anhydrase ii complexed with 4-(aminosulfonyl)-n-[(2,3-difluorophenyl)methyl]-benzamide
S +31 S 22x +31 1hcaA Unexpected ph-dependent conformation of his-64, the proton shuttle of carbonic anhydrase ii.
S +31 S 11x +31 1hebA Structural consequences of hydrophilic amino-acid substitutions in the hydrophobic pocket of human carbonic anhydrase ii
S +31 S 19x +31 1hedA Structural consequences of hydrophilic amino-acid substitutions in the hydrophobic pocket of human carbonic anhydrase ii
S +31 S 11x +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 S 7x +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 S 23x +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 S 7x +31 1i9mA Carbonic anhydrase ii (f131v) complexed with 4-(aminosulfonyl)-n-[(2,4-difluorophenyl)methyl]-benzamide
S +31 S 19x +31 1i9oA Carbonic anhydrase ii (f131v) complexed with 4-(aminosulfonyl)-n-[(2,3,4-trifluorophenyl)methyl]-benzamide
S +31 S 19x +31 1i9pA Carbonic anhydrase ii (f131v) complexed with 4-(aminosulfonyl)-n-[(2,4,6-trifluorophenyl)methyl]-benzamide
S +31 S 23x +31 1if5A Carbonic anhydrase ii complexed with 2,6-difluorobenzenesulfonamide
K +31 K 23x +31 1if7A Carbonic anhydrase ii complexed with (r)-n-(3-indol-1-yl-2-methyl-propyl)-4-sulfamoyl-benzamide
S +31 S 11x +31 1if8A Carbonic anhydrase ii complexed with (s)-n-(3-indol-1-yl-2-methyl-propyl)-4-sulfamoyl-benzamide
K +31 K 23x +31 1if9A Carbonic anhydrase ii complexed with n-[2-(1h-indol-5-yl)-butyl]-4-sulfamoyl-benzamide
S +31 S 3x +31 1jd0A Crystal structure of the extracellular domain of human carbonic anhydrase xii complexed with acetazolamide
S +31 S 15x +31 1kwqA Human carbonic anhydrase ii complexed with inhibitor 2000-07
K +31 K 1x +31 1thkA Effect of shuttle location and ph environment on h+ transfer in human carbonic anhydrase ii
S +31 S 1x +31 1v9eA Crystal structure analysis of bovine carbonic anhydrase ii
S +31 S 15x +31 1ydcA Structural basis of inhibitor affinity to variants of human carbonic anhydrase ii
S +31 S 10x +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 S 3x +31 2cbbA Structure of native and apo carbonic anhydrase ii and some of its anion-ligand complexes
K +31 K 7x +31 2cbcA Structure of native and apo carbonic anhydrase ii and some of its anion-ligand complexes
K +31 K 7x +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 S 11x +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 S 3x +31
4
2fouA Human carbonic anhydrase ii complexed with two-prong inhibitors
S +31 S 3x +31 2nwyA Structural and kinetic effects of hydrophobic mutations on the active site of human carbonic anhydrase ii
K +31 K 3x +31 2osfA Inhibition of carbonic anhydrase ii by thioxolone: a mechanistic and structural study
S +31 S 15x +31 6ca2A Engineering the hydrophobic pocket of carbonic anhydrase ii
S +31 S 7x +31 2o4zA Crystal structure of the carbonic anhydrase ii complexed with hydroxysulfamide inhibitor
S +31 S 3x +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 S 22x +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 S 23x +31 3f8eA Coumarins are a novel class of suicide carbonic anhydrase inhibitors
S +31 S 22x +31 1ydaA Structural basis of inhibitor affinity to variants of human carbonic anhydrase ii
S +31 S 11x +31 2q1qA Carbonic anhydrase inhibitors. interaction of the antiepileptic drug sulthiame with twelve mammalian isoforms: kinetic and x-ray crystallographic studies
S +31 S 3x +31 2wegA Thermodynamic optimisation of carbonic anhydrase fragment inhibitors
K +31 K 3x +31 3bl0A Carbonic anhydrase inhibitors. interaction of 2-n,n-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide with twelve mammalian isoforms: kinetic and x-ray crystallographic studies
K +31 K 3x +31 3czvA Crystal structure of the human carbonic anhydrase xiii in complex with acetazolamide
S +31 S 3x +31 3d0nA Crystal structure of human carbonic anhydrase xiii
S +31 S 3x +31 3dbuA Use of carbonic anhydrase ii, ix active-site mimic, for the purpose of screening inhibitors for possible anti-cancer properties
S +31 S 3x +31 3efiA Carbonic anhydrase activators: kinetic and x-ray crystallographic study for the interaction of d- and l-tryptophan with the mammalian isoforms i-xiv
S +31 S 3x +31
4
3eftA Crystal structure of the complex between carbonic anhydrase ii and a spin-labeled sulfonamide incorporating tempo moiety
S +31 S 3x +31 3kokA Crystal structure of cobalt (ii) human carbonic anhydrase ii at ph 8.5
K +31 K 3x +31 3okvA Human carbonic anhydrase ii a65s, n67q (ca ix mimic) bound with 2-ethylestrone 3-o-sulfamate
S +31 S 3x +31 3ffpX X ray structure of the complex between carbonic anhydrase ii and lc inhibitors
S +31 S 3x +31 1bcdA X-ray crystallographic structure of a complex between human carbonic anhydrase ii and a new topical inhibitor, trifluoromethane sulphonamide
S +31 S 11x +31 1bicA Crystallographic analysis of thr-200-> his human carbonic anhydrase ii and its complex with the substrate, hco3-
S +31 S 15x +31 1canA Crystallographic studies of the binding of protonated and unprotonated inhibitors to carbonic anhydrase using hydrogen sulphide and nitrate anions
S +31 S 20x +31 1cinA The positions of his-64 and a bound water in human carbonic anhydrase ii upon binding three structurally related inhibitors
S +31 S 15x +31 1craA The complex between human carbonic anhydrase ii and the aromatic inhibitor 1,2,4-triazole
S +31 S 31x +31 1czmA Drug-protein interactions: structure of sulfonamide drug complexed with human carbonic anhydrase i
K +31 K 23x +31 1fqmA X-ray crystal structure of zinc-bound f93i/f95m/w97v carbonic anhydrase (caii) variant
S +31 S 8x +31 1jv0A The crystal structure of the zinc(ii) adduct of the cai michigan 1 variant
S +31 S 2x +31 1kopA Neisseria gonorrhoeae carbonic anhydrase

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