eF-site ID 5l3o-A PDB Code 5l3o Chain A click to enlarge Title Crystal Structure of Human Carbonic Anhydrase II in Complex with a Quinoline Oligoamide Foldamer Classification Lyase/Inhibitor Compound Carbonic anhydrase 2 Source (CAH2_HUMAN) Sequence A:  SHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYD PSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKG GPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLV HWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVD VLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPP LLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMV DNWRPAQPLKNRQIKASFK Description Functional site 1) chain A residue 94 type sequence H description binding site for residue ZN A 301 source : AC1 2) chain A residue 96 type sequence H description binding site for residue ZN A 301 source : AC1 3) chain A residue 119 type sequence H description binding site for residue ZN A 301 source : AC1 4) chain A residue 62 type sequence N description binding site for residue GOL A 306 source : AC2 5) chain A residue 67 type sequence N description binding site for residue GOL A 306 source : AC2 6) chain A residue 92 type sequence Q description binding site for residue GOL A 306 source : AC2 7) chain A residue 94 type sequence H description binding site for residue GOL A 306 source : AC2 8) chain A residue 96 type sequence H description binding site for residue GOL A 306 source : AC2 9) chain A residue 4 type sequence H description binding site for residue GOL A 307 source : AC3 10) chain A residue 11 type sequence N description binding site for residue GOL A 307 source : AC3 11) chain A residue 15 type sequence H description binding site for residue GOL A 307 source : AC3 12) chain A residue 16 type sequence W description binding site for residue GOL A 307 source : AC3 13) chain A residue 18 type sequence K description binding site for residue GOL A 307 source : AC3 14) chain A residue 19 type sequence D description binding site for residue GOL A 307 source : AC3 15) chain A residue 7 type sequence Y description binding site for residue GOL A 308 source : AC4 16) chain A residue 242 type sequence D description binding site for residue GOL A 308 source : AC4 17) chain A residue 244 type sequence W description binding site for residue GOL A 308 source : AC4 18) chain A residue 246 type sequence P description binding site for residue GOL A 308 source : AC4 19) chain A residue 94 type sequence H description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 20) chain A residue 96 type sequence H description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 21) chain A residue 119 type sequence H description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 22) chain A residue 130 type sequence F description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 23) chain A residue 142 type sequence V description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 24) chain A residue 197 type sequence L description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 25) chain A residue 198 type sequence T description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 26) chain A residue 199 type sequence T description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 27) chain A residue 201 type sequence P description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 28) chain A residue 208 type sequence W description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 29) chain A residue 3 type sequence H description binding site for residues QUK A 303 and QVS A 304 source : AD4 30) chain A residue 20 type sequence F description binding site for residues QUK A 303 and QVS A 304 source : AD4 31) chain A residue 3 type sequence H description binding site for residues QUK A 303 and QUJ A 312 source : AD5 32) chain A residue 2 type sequence S description binding site for residues QVS A 304 and QVE A 305 source : AD6 33) chain A residue 3 type sequence H description binding site for residues QVS A 304 and QVE A 305 source : AD6 34) chain A residue 20 type sequence F description binding site for residues QVS A 304 and QVE A 305 source : AD6 35) chain A residue 94 type sequence H description binding site for residues QUJ A 310 and QUK B 301 source : AE1 36) chain A residue 96 type sequence H description binding site for residues QUJ A 310 and QUK B 301 source : AE1 37) chain A residue 119 type sequence H description binding site for residues QUJ A 310 and QUK B 301 source : AE1 38) chain A residue 129 type sequence D description binding site for residues QUJ A 310 and QUK B 301 source : AE1 39) chain A residue 132 type sequence K description binding site for residues QUJ A 310 and QUK B 301 source : AE1 40) chain A residue 94 type sequence H description binding site for residues QVS A 311 and QVE B 302 source : AE2 41) chain A residue 96 type sequence H description binding site for residues QVS A 311 and QVE B 302 source : AE2 42) chain A residue 119 type sequence H description binding site for residues QVS A 311 and QVE B 302 source : AE2 43) chain A residue 130 type sequence F description binding site for residues QVS A 311 and QVE B 302 source : AE2 44) chain A residue 142 type sequence V description binding site for residues QVS A 311 and QVE B 302 source : AE2 45) chain A residue 197 type sequence L description binding site for residues QVS A 311 and QVE B 302 source : AE2 46) chain A residue 198 type sequence T description binding site for residues QVS A 311 and QVE B 302 source : AE2 47) chain A residue 199 type sequence T description binding site for residues QVS A 311 and QVE B 302 source : AE2 48) chain A residue 201 type sequence P description binding site for residues QVS A 311 and QVE B 302 source : AE2 49) chain A residue 208 type sequence W description binding site for residues QVS A 311 and QVE B 302 source : AE2 50) chain A residue 94 type sequence H description binding site for residues QVS A 311 and QUK B 301 source : AE3 51) chain A residue 96 type sequence H description binding site for residues QVS A 311 and QUK B 301 source : AE3 52) chain A residue 119 type sequence H description binding site for residues QVS A 311 and QUK B 301 source : AE3 53) chain A residue 131 type sequence G description binding site for residues QUJ B 303 and 6H0 B 308 source : AE7 54) chain A residue 131 type sequence G description binding site for residues QUJ B 303 and QUK B 309 source : AE8 55) chain A residue 129 type sequence D description binding site for residues QUK B 309 and QVS B 310 source : AF1 56) chain A residue 132 type sequence K description binding site for residues QUK B 309 and QVS B 310 source : AF1 57) chain A residue 129 type sequence D description binding site for residues QVS B 310 and QVE B 311 source : AF2 58) chain A residue 132 type sequence K description binding site for residues QVS B 310 and QVE B 311 source : AF2 59) chain A residue 64 type catalytic sequence H description 216 source MCSA : MCSA1 60) chain A residue 94 type catalytic sequence H description 216 source MCSA : MCSA1 61) chain A residue 96 type catalytic sequence H description 216 source MCSA : MCSA1 62) chain A residue 106 type catalytic sequence E description 216 source MCSA : MCSA1 63) chain A residue 119 type catalytic sequence H description 216 source MCSA : MCSA1 64) chain A residue 198 type catalytic sequence T description 216 source MCSA : MCSA1 65) chain A 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 66) chain A residue 2 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P27139 source Swiss-Prot : SWS_FT_FI8 67) chain A 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 68) chain A 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 69) chain A 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 70) chain A 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 71) chain A residue 105-121 type prosite sequence SEHTVDKKKYAAELHLV description ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV source prosite : PS00162 72) chain A 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 73) chain A residue 165 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 74) chain A residue 172 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 75) chain A 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 76) chain A 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 77) chain A residue 198 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834 source Swiss-Prot : SWS_FT_FI4

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