eF-site ID 5l6k-B PDB Code 5l6k Chain B click to enlarge Title Crystal Structure of Human Carbonic Anhydrase II in Complex with a Quinoline Oligoamide Foldamer Classification LYASE Compound Carbonic anhydrase 2 Source (CAH2_HUMAN) Sequence B:  SHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYD PSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKG GPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLV HWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVD VLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPP LLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMV DNWRPAQPLKNRQIKASFK Description Functional site 1) chain B residue 94 type sequence H description binding site for residue ZN B 305 source : AC9 2) chain B residue 96 type sequence H description binding site for residue ZN B 305 source : AC9 3) chain B residue 119 type sequence H description binding site for residue ZN B 305 source : AC9 4) chain B residue 62 type sequence N description binding site for residue GOL B 312 source : AD3 5) chain B residue 64 type sequence H description binding site for residue GOL B 312 source : AD3 6) chain B residue 67 type sequence N description binding site for residue GOL B 312 source : AD3 7) chain B residue 92 type sequence Q description binding site for residue GOL B 312 source : AD3 8) chain B residue 199 type sequence T description binding site for residue GOL B 312 source : AD3 9) chain B residue 67 type sequence N description binding site for residue GOL B 313 source : AD4 10) chain B residue 69 type sequence E description binding site for residue GOL B 313 source : AD4 11) chain B residue 92 type sequence Q description binding site for residue GOL B 313 source : AD4 12) chain B residue 131 type sequence G description binding site for residues 6H0 A 302 and QUJ A 315 source : AD5 13) chain B residue 129 type sequence D description binding site for residues QUK A 303 and QVS A 304 source : AD6 14) chain B residue 132 type sequence K description binding site for residues QUK A 303 and QVS A 304 source : AD6 15) chain B residue 131 type sequence G description binding site for residues QUK A 303 and QUJ A 315 source : AD7 16) chain B residue 129 type sequence D description binding site for residues QVS A 304 and QVE A 305 source : AD8 17) chain B residue 132 type sequence K description binding site for residues QVS A 304 and QVE A 305 source : AD8 18) chain B residue 94 type sequence H description binding site for residues QUK A 306 and QVS B 304 source : AD9 19) chain B residue 96 type sequence H description binding site for residues QUK A 306 and QVS B 304 source : AD9 20) chain B residue 119 type sequence H description binding site for residues QUK A 306 and QVS B 304 source : AD9 21) chain B residue 129 type sequence D description binding site for residues QUK A 306 and QVS B 304 source : AD9 22) chain B residue 130 type sequence F description binding site for residues QUK A 306 and QVS B 304 source : AD9 23) chain B residue 132 type sequence K description binding site for residues QUK A 306 and QVS B 304 source : AD9 24) chain B residue 142 type sequence V description binding site for residues QUK A 306 and QVS B 304 source : AD9 25) chain B residue 197 type sequence L description binding site for residues QUK A 306 and QVS B 304 source : AD9 26) chain B residue 198 type sequence T description binding site for residues QUK A 306 and QVS B 304 source : AD9 27) chain B residue 199 type sequence T description binding site for residues QUK A 306 and QVS B 304 source : AD9 28) chain B residue 201 type sequence P description binding site for residues QUK A 306 and QVS B 304 source : AD9 29) chain B residue 208 type sequence W description binding site for residues QUK A 306 and QVS B 304 source : AD9 30) chain B residue 94 type sequence H description binding site for residues QUK A 306 and QUJ B 303 source : AE1 31) chain B residue 96 type sequence H description binding site for residues QUK A 306 and QUJ B 303 source : AE1 32) chain B residue 119 type sequence H description binding site for residues QUK A 306 and QUJ B 303 source : AE1 33) chain B residue 130 type sequence F description binding site for residues QUK A 306 and QUJ B 303 source : AE1 34) chain B residue 142 type sequence V description binding site for residues QUK A 306 and QUJ B 303 source : AE1 35) chain B residue 197 type sequence L description binding site for residues QUK A 306 and QUJ B 303 source : AE1 36) chain B residue 198 type sequence T description binding site for residues QUK A 306 and QUJ B 303 source : AE1 37) chain B residue 199 type sequence T description binding site for residues QUK A 306 and QUJ B 303 source : AE1 38) chain B residue 201 type sequence P description binding site for residues QUK A 306 and QUJ B 303 source : AE1 39) chain B residue 208 type sequence W description binding site for residues QUK A 306 and QUJ B 303 source : AE1 40) chain B residue 2 type sequence S description binding site for residues QVE A 307 and QVS B 304 source : AE2 41) chain B residue 3 type sequence H description binding site for residues QVE A 307 and QVS B 304 source : AE2 42) chain B residue 129 type sequence D description binding site for residues QVE A 307 and QVS B 304 source : AE2 43) chain B residue 132 type sequence K description binding site for residues QVE A 307 and QVS B 304 source : AE2 44) chain B residue 94 type sequence H description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 45) chain B residue 96 type sequence H description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 46) chain B residue 119 type sequence H description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 47) chain B residue 130 type sequence F description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 48) chain B residue 142 type sequence V description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 49) chain B residue 197 type sequence L description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 50) chain B residue 198 type sequence T description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 51) chain B residue 199 type sequence T description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 52) chain B residue 201 type sequence P description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 53) chain B residue 208 type sequence W description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 54) chain B residue 2 type sequence S description binding site for residues QUJ B 301 and QUK B 307 source : AE4 55) chain B residue 3 type sequence H description binding site for residues QUJ B 301 and QUK B 307 source : AE4 56) chain B residue 2 type sequence S description binding site for residues QUK B 307 and QVS B 308 source : AE6 57) chain B residue 3 type sequence H description binding site for residues QUK B 307 and QVS B 308 source : AE6 58) chain B residue 19 type sequence D description binding site for residues QUK B 307 and QVS B 308 source : AE6 59) chain B residue 20 type sequence F description binding site for residues QUK B 307 and QVS B 308 source : AE6 60) chain B residue 2 type sequence S description binding site for residues QVS B 308 and QVE B 309 source : AE7 61) chain B residue 3 type sequence H description binding site for residues QVS B 308 and QVE B 309 source : AE7 62) chain B residue 19 type sequence D description binding site for residues QVS B 308 and QVE B 309 source : AE7 63) chain B residue 20 type sequence F description binding site for residues QVS B 308 and QVE B 309 source : AE7 64) chain B residue 64 type catalytic sequence H description 216 source MCSA : MCSA2 65) chain B residue 94 type catalytic sequence H description 216 source MCSA : MCSA2 66) chain B residue 96 type catalytic sequence H description 216 source MCSA : MCSA2 67) chain B residue 106 type catalytic sequence E description 216 source MCSA : MCSA2 68) chain B residue 119 type catalytic sequence H description 216 source MCSA : MCSA2 69) chain B residue 198 type catalytic sequence T description 216 source MCSA : MCSA2 70) chain B residue 94 type BINDING sequence H description BINDING => ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:4621826, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942 source Swiss-Prot : SWS_FT_FI2 71) chain B residue 198 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834 source Swiss-Prot : SWS_FT_FI4 72) chain B residue 92 type SITE sequence Q description Involved in the binding of some activators, including histamine and L-histidine => ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962 source Swiss-Prot : SWS_FT_FI7 73) chain B residue 7 type SITE sequence Y description Fine-tunes the proton-transfer properties of H-64 => ECO:0000305|PubMed:17330962 source Swiss-Prot : SWS_FT_FI5 74) chain B residue 62 type SITE sequence N description Fine-tunes the proton-transfer properties of H-64; involved in the binding of some activators, including histamine and L-histidine => ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962 source Swiss-Prot : SWS_FT_FI6 75) chain B residue 67 type SITE sequence N description Fine-tunes the proton-transfer properties of H-64; involved in the binding of some activators, including histamine and L-histidine => ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962 source Swiss-Prot : SWS_FT_FI6 76) chain B residue 64 type ACT_SITE sequence H description Proton donor/acceptor => ECO:0000305|PubMed:15667203, ECO:0000305|PubMed:17330962 source Swiss-Prot : SWS_FT_FI1 77) chain B residue 165 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 78) chain B residue 172 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 79) chain B residue 96 type BINDING sequence H description BINDING => ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942 source Swiss-Prot : SWS_FT_FI3 80) chain B residue 119 type BINDING sequence H description BINDING => ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942 source Swiss-Prot : SWS_FT_FI3 81) chain B residue 2 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P27139 source Swiss-Prot : SWS_FT_FI8

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