eF-site ID 5l6k-AB PDB Code 5l6k Chain A, 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 (5L6K) Sequence A:  SHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYD PSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKG GPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLV HWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVD VLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPP LLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMV DNWRPAQPLKNRQIKASFK B:  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 302 source : AC2 5) chain A residue 65 type sequence A description binding site for residue GOL A 302 source : AC2 6) chain A residue 67 type sequence N description binding site for residue GOL A 302 source : AC2 7) chain A residue 92 type sequence Q description binding site for residue GOL A 302 source : AC2 8) chain A residue 94 type sequence H description binding site for residue GOL A 302 source : AC2 9) chain A residue 199 type sequence T description binding site for residue GOL A 302 source : AC2 10) chain A residue 67 type sequence N description binding site for residue GOL A 303 source : AC3 11) chain A residue 69 type sequence E description binding site for residue GOL A 303 source : AC3 12) chain A residue 92 type sequence Q description binding site for residue GOL A 303 source : AC3 13) chain A residue 130 type sequence F description binding site for residue GOL A 303 source : AC3 14) chain A residue 32 type sequence D description binding site for residue NA A 304 source : AC7 15) chain A residue 110 type sequence D description binding site for residue NA A 304 source : AC7 16) chain A residue 11 type sequence N description binding site for residue DMS A 305 source : AC8 17) chain A residue 15 type sequence H description binding site for residue DMS A 305 source : AC8 18) chain A residue 16 type sequence W description binding site for residue DMS A 305 source : AC8 19) chain A residue 18 type sequence K description binding site for residue DMS A 305 source : AC8 20) chain A residue 19 type sequence D description binding site for residue DMS A 305 source : AC8 21) chain B residue 94 type sequence H description binding site for residue ZN B 301 source : AC9 22) chain B residue 96 type sequence H description binding site for residue ZN B 301 source : AC9 23) chain B residue 119 type sequence H description binding site for residue ZN B 301 source : AC9 24) chain B residue 62 type sequence N description binding site for residue GOL B 302 source : AD3 25) chain B residue 64 type sequence H description binding site for residue GOL B 302 source : AD3 26) chain B residue 67 type sequence N description binding site for residue GOL B 302 source : AD3 27) chain B residue 92 type sequence Q description binding site for residue GOL B 302 source : AD3 28) chain B residue 199 type sequence T description binding site for residue GOL B 302 source : AD3 29) chain B residue 67 type sequence N description binding site for residue GOL B 303 source : AD4 30) chain B residue 69 type sequence E description binding site for residue GOL B 303 source : AD4 31) chain B residue 92 type sequence Q description binding site for residue GOL B 303 source : AD4 32) chain A residue 3 type sequence H description binding site for residues QUK A 303 and QVS A 304 source : AD6 33) chain A residue 19 type sequence D description binding site for residues QUK A 303 and QVS A 304 source : AD6 34) chain A residue 20 type sequence F description binding site for residues QUK A 303 and QVS A 304 source : AD6 35) chain B residue 129 type sequence D description binding site for residues QUK A 303 and QVS A 304 source : AD6 36) chain B residue 132 type sequence K description binding site for residues QUK A 303 and QVS A 304 source : AD6 37) chain A residue 3 type sequence H description binding site for residues QUK A 303 and QUJ A 315 source : AD7 38) chain B residue 131 type sequence G description binding site for residues QUK A 303 and QUJ A 315 source : AD7 39) chain A residue 2 type sequence S description binding site for residues QVS A 304 and QVE A 305 source : AD8 40) chain A residue 3 type sequence H description binding site for residues QVS A 304 and QVE A 305 source : AD8 41) chain A residue 19 type sequence D description binding site for residues QVS A 304 and QVE A 305 source : AD8 42) chain A residue 20 type sequence F description binding site for residues QVS A 304 and QVE A 305 source : AD8 43) chain B residue 129 type sequence D description binding site for residues QVS A 304 and QVE A 305 source : AD8 44) chain B residue 132 type sequence K description binding site for residues QVS A 304 and QVE A 305 source : AD8 45) chain A residue 130 type sequence F description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 46) chain A residue 131 type sequence G description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 47) chain B residue 94 type sequence H description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 48) chain B residue 96 type sequence H description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 49) chain B residue 119 type sequence H description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 50) chain B residue 130 type sequence F description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 51) chain B residue 142 type sequence V description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 52) chain B residue 197 type sequence L description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 53) chain B residue 198 type sequence T description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 54) chain B residue 199 type sequence T description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 55) chain B residue 201 type sequence P description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 56) chain B residue 208 type sequence W description binding site for residues QUJ B 301 and 6H0 B 306 source : AE3 57) chain A residue 130 type sequence F description binding site for residues QUJ B 301 and QUK B 307 source : AE4 58) chain A residue 131 type sequence G description binding site for residues QUJ B 301 and QUK B 307 source : AE4 59) chain B residue 2 type sequence S description binding site for residues QUJ B 301 and QUK B 307 source : AE4 60) chain B residue 3 type sequence H description binding site for residues QUJ B 301 and QUK B 307 source : AE4 61) chain A residue 129 type sequence D description binding site for residues QUK B 307 and QVS B 308 source : AE6 62) chain A residue 132 type sequence K description binding site for residues QUK B 307 and QVS B 308 source : AE6 63) chain B residue 2 type sequence S description binding site for residues QUK B 307 and QVS B 308 source : AE6 64) chain B residue 3 type sequence H description binding site for residues QUK B 307 and QVS B 308 source : AE6 65) chain B residue 19 type sequence D description binding site for residues QUK B 307 and QVS B 308 source : AE6 66) chain B residue 20 type sequence F description binding site for residues QUK B 307 and QVS B 308 source : AE6 67) chain A residue 129 type sequence D description binding site for residues QVS B 308 and QVE B 309 source : AE7 68) chain A residue 132 type sequence K description binding site for residues QVS B 308 and QVE B 309 source : AE7 69) chain B residue 2 type sequence S description binding site for residues QVS B 308 and QVE B 309 source : AE7 70) chain B residue 3 type sequence H description binding site for residues QVS B 308 and QVE B 309 source : AE7 71) chain B residue 19 type sequence D description binding site for residues QVS B 308 and QVE B 309 source : AE7 72) chain B residue 20 type sequence F description binding site for residues QVS B 308 and QVE B 309 source : AE7 73) chain A residue 64 type catalytic sequence H description 216 source MCSA : MCSA1 74) chain A residue 94 type catalytic sequence H description 216 source MCSA : MCSA1 75) chain A residue 96 type catalytic sequence H description 216 source MCSA : MCSA1 76) chain A residue 106 type catalytic sequence E description 216 source MCSA : MCSA1 77) chain A residue 119 type catalytic sequence H description 216 source MCSA : MCSA1 78) chain A residue 198 type catalytic sequence T description 216 source MCSA : MCSA1 79) chain B residue 64 type catalytic sequence H description 216 source MCSA : MCSA2 80) chain B residue 94 type catalytic sequence H description 216 source MCSA : MCSA2 81) chain B residue 96 type catalytic sequence H description 216 source MCSA : MCSA2 82) chain B residue 106 type catalytic sequence E description 216 source MCSA : MCSA2 83) chain B residue 119 type catalytic sequence H description 216 source MCSA : MCSA2 84) chain B residue 198 type catalytic sequence T description 216 source MCSA : MCSA2 85) chain A residue 105-121 type prosite sequence SEHTVDKKKYAAELHLV description ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV source prosite : PS00162 86) 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 87) 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 88) 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 89) 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 90) 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 91) 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 92) 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 93) 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 94) chain A residue 198 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834 source Swiss-Prot : SWS_FT_FI4 95) chain B residue 198 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834 source Swiss-Prot : SWS_FT_FI4 96) 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 97) 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 98) 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 99) 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 100) 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 101) 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 102) 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 103) 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 104) chain A residue 2 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P27139 source Swiss-Prot : SWS_FT_FI8 105) chain B residue 2 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P27139 source Swiss-Prot : SWS_FT_FI8 106) chain A residue 165 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 107) chain A residue 172 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 108) chain B residue 165 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 109) chain B residue 172 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9

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