eF-site ID 5l3o-AB PDB Code 5l3o Chain A, B 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 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 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 B residue 94 type sequence H description binding site for residue ZN B 307 source : AC7 20) chain B residue 96 type sequence H description binding site for residue ZN B 307 source : AC7 21) chain B residue 119 type sequence H description binding site for residue ZN B 307 source : AC7 22) chain B residue 7 type sequence Y description binding site for residue GOL B 312 source : AC8 23) chain B residue 62 type sequence N description binding site for residue GOL B 312 source : AC8 24) chain B residue 64 type sequence H description binding site for residue GOL B 312 source : AC8 25) chain B residue 65 type sequence A description binding site for residue GOL B 312 source : AC8 26) chain B residue 67 type sequence N description binding site for residue GOL B 312 source : AC8 27) chain B residue 92 type sequence Q description binding site for residue GOL B 312 source : AC8 28) chain B residue 94 type sequence H description binding site for residue GOL B 312 source : AC8 29) chain B residue 96 type sequence H description binding site for residue GOL B 312 source : AC8 30) chain B residue 199 type sequence T description binding site for residue GOL B 312 source : AC8 31) chain B residue 4 type sequence H description binding site for residue GOL B 313 source : AC9 32) chain B residue 11 type sequence N description binding site for residue GOL B 313 source : AC9 33) chain B residue 15 type sequence H description binding site for residue GOL B 313 source : AC9 34) chain B residue 16 type sequence W description binding site for residue GOL B 313 source : AC9 35) chain B residue 18 type sequence K description binding site for residue GOL B 313 source : AC9 36) chain B residue 19 type sequence D description binding site for residue GOL B 313 source : AC9 37) chain B residue 7 type sequence Y description binding site for residue GOL B 314 source : AD1 38) chain B residue 242 type sequence D description binding site for residue GOL B 314 source : AD1 39) chain B residue 244 type sequence W description binding site for residue GOL B 314 source : AD1 40) chain B residue 246 type sequence P description binding site for residue GOL B 314 source : AD1 41) chain B residue 163 type sequence L description binding site for residue GOL B 315 source : AD2 42) chain B residue 164 type sequence D description binding site for residue GOL B 315 source : AD2 43) chain B residue 167 type sequence K description binding site for residue GOL B 315 source : AD2 44) chain B residue 224 type sequence K description binding site for residue GOL B 315 source : AD2 45) chain B residue 227 type sequence K description binding site for residue GOL B 315 source : AD2 46) chain B residue 228 type sequence L description binding site for residue GOL B 315 source : AD2 47) chain A residue 94 type sequence H description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 48) chain A residue 96 type sequence H description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 49) chain A residue 119 type sequence H description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 50) chain A residue 130 type sequence F description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 51) chain A residue 142 type sequence V description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 52) chain A residue 197 type sequence L description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 53) chain A residue 198 type sequence T description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 54) chain A residue 199 type sequence T description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 55) chain A residue 201 type sequence P description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 56) chain A residue 208 type sequence W description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 57) chain B residue 131 type sequence G description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 58) chain A residue 3 type sequence H description binding site for residues QUK A 303 and QVS A 304 source : AD4 59) chain A residue 20 type sequence F description binding site for residues QUK A 303 and QVS A 304 source : AD4 60) chain B residue 129 type sequence D description binding site for residues QUK A 303 and QVS A 304 source : AD4 61) chain B residue 132 type sequence K description binding site for residues QUK A 303 and QVS A 304 source : AD4 62) chain A residue 3 type sequence H description binding site for residues QUK A 303 and QUJ A 312 source : AD5 63) chain B residue 131 type sequence G description binding site for residues QUK A 303 and QUJ A 312 source : AD5 64) chain A residue 2 type sequence S description binding site for residues QVS A 304 and QVE A 305 source : AD6 65) chain A residue 3 type sequence H description binding site for residues QVS A 304 and QVE A 305 source : AD6 66) chain A residue 20 type sequence F description binding site for residues QVS A 304 and QVE A 305 source : AD6 67) chain B residue 129 type sequence D description binding site for residues QVS A 304 and QVE A 305 source : AD6 68) chain B residue 132 type sequence K description binding site for residues QVS A 304 and QVE A 305 source : AD6 69) chain A residue 94 type sequence H description binding site for residues QUJ A 310 and QUK B 301 source : AE1 70) chain A residue 96 type sequence H description binding site for residues QUJ A 310 and QUK B 301 source : AE1 71) chain A residue 119 type sequence H description binding site for residues QUJ A 310 and QUK B 301 source : AE1 72) chain A residue 129 type sequence D description binding site for residues QUJ A 310 and QUK B 301 source : AE1 73) chain A residue 132 type sequence K description binding site for residues QUJ A 310 and QUK B 301 source : AE1 74) chain B residue 3 type sequence H description binding site for residues QUJ A 310 and QUK B 301 source : AE1 75) chain B residue 19 type sequence D description binding site for residues QUJ A 310 and QUK B 301 source : AE1 76) chain B residue 20 type sequence F description binding site for residues QUJ A 310 and QUK B 301 source : AE1 77) chain A residue 94 type sequence H description binding site for residues QVS A 311 and QVE B 302 source : AE2 78) chain A residue 96 type sequence H description binding site for residues QVS A 311 and QVE B 302 source : AE2 79) chain A residue 119 type sequence H description binding site for residues QVS A 311 and QVE B 302 source : AE2 80) chain A residue 130 type sequence F description binding site for residues QVS A 311 and QVE B 302 source : AE2 81) chain A residue 142 type sequence V description binding site for residues QVS A 311 and QVE B 302 source : AE2 82) chain A residue 197 type sequence L description binding site for residues QVS A 311 and QVE B 302 source : AE2 83) chain A residue 198 type sequence T description binding site for residues QVS A 311 and QVE B 302 source : AE2 84) chain A residue 199 type sequence T description binding site for residues QVS A 311 and QVE B 302 source : AE2 85) chain A residue 201 type sequence P description binding site for residues QVS A 311 and QVE B 302 source : AE2 86) chain A residue 208 type sequence W description binding site for residues QVS A 311 and QVE B 302 source : AE2 87) chain B residue 2 type sequence S description binding site for residues QVS A 311 and QVE B 302 source : AE2 88) chain B residue 3 type sequence H description binding site for residues QVS A 311 and QVE B 302 source : AE2 89) chain A residue 94 type sequence H description binding site for residues QVS A 311 and QUK B 301 source : AE3 90) chain A residue 96 type sequence H description binding site for residues QVS A 311 and QUK B 301 source : AE3 91) chain A residue 119 type sequence H description binding site for residues QVS A 311 and QUK B 301 source : AE3 92) chain B residue 2 type sequence S description binding site for residues QVS A 311 and QUK B 301 source : AE3 93) chain B residue 3 type sequence H description binding site for residues QVS A 311 and QUK B 301 source : AE3 94) chain A residue 131 type sequence G description binding site for residues QUJ B 303 and 6H0 B 308 source : AE7 95) chain B residue 94 type sequence H description binding site for residues QUJ B 303 and 6H0 B 308 source : AE7 96) chain B residue 96 type sequence H description binding site for residues QUJ B 303 and 6H0 B 308 source : AE7 97) chain B residue 119 type sequence H description binding site for residues QUJ B 303 and 6H0 B 308 source : AE7 98) chain B residue 130 type sequence F description binding site for residues QUJ B 303 and 6H0 B 308 source : AE7 99) chain B residue 197 type sequence L description binding site for residues QUJ B 303 and 6H0 B 308 source : AE7 100) chain B residue 198 type sequence T description binding site for residues QUJ B 303 and 6H0 B 308 source : AE7 101) chain B residue 199 type sequence T description binding site for residues QUJ B 303 and 6H0 B 308 source : AE7 102) chain B residue 201 type sequence P description binding site for residues QUJ B 303 and 6H0 B 308 source : AE7 103) chain B residue 208 type sequence W description binding site for residues QUJ B 303 and 6H0 B 308 source : AE7 104) chain A residue 131 type sequence G description binding site for residues QUJ B 303 and QUK B 309 source : AE8 105) chain B residue 3 type sequence H description binding site for residues QUJ B 303 and QUK B 309 source : AE8 106) chain B residue 135 type sequence Q description binding site for residues 6H0 B 304 and QUJ B 305 source : AE9 107) chain A residue 129 type sequence D description binding site for residues QUK B 309 and QVS B 310 source : AF1 108) chain A residue 132 type sequence K description binding site for residues QUK B 309 and QVS B 310 source : AF1 109) chain B residue 3 type sequence H description binding site for residues QUK B 309 and QVS B 310 source : AF1 110) chain B residue 19 type sequence D description binding site for residues QUK B 309 and QVS B 310 source : AF1 111) chain B residue 20 type sequence F description binding site for residues QUK B 309 and QVS B 310 source : AF1 112) chain A residue 129 type sequence D description binding site for residues QVS B 310 and QVE B 311 source : AF2 113) chain A residue 132 type sequence K description binding site for residues QVS B 310 and QVE B 311 source : AF2 114) chain B residue 2 type sequence S description binding site for residues QVS B 310 and QVE B 311 source : AF2 115) chain B residue 3 type sequence H description binding site for residues QVS B 310 and QVE B 311 source : AF2 116) chain B residue 19 type sequence D description binding site for residues QVS B 310 and QVE B 311 source : AF2 117) chain B residue 20 type sequence F description binding site for residues QVS B 310 and QVE B 311 source : AF2 118) chain A residue 64 type catalytic sequence H description 216 source MCSA : MCSA1 119) chain A residue 94 type catalytic sequence H description 216 source MCSA : MCSA1 120) chain A residue 96 type catalytic sequence H description 216 source MCSA : MCSA1 121) chain A residue 106 type catalytic sequence E description 216 source MCSA : MCSA1 122) chain A residue 119 type catalytic sequence H description 216 source MCSA : MCSA1 123) chain A residue 198 type catalytic sequence T description 216 source MCSA : MCSA1 124) chain B residue 64 type catalytic sequence H description 216 source MCSA : MCSA2 125) chain B residue 94 type catalytic sequence H description 216 source MCSA : MCSA2 126) chain B residue 96 type catalytic sequence H description 216 source MCSA : MCSA2 127) chain B residue 106 type catalytic sequence E description 216 source MCSA : MCSA2 128) chain B residue 119 type catalytic sequence H description 216 source MCSA : MCSA2 129) chain B residue 198 type catalytic sequence T description 216 source MCSA : MCSA2 130) 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 131) 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 132) chain A residue 2 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P27139 source Swiss-Prot : SWS_FT_FI8 133) chain B residue 2 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P27139 source Swiss-Prot : SWS_FT_FI8 134) 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 135) 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 136) 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 137) 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 138) 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 139) 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 140) 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 141) 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 142) chain A residue 105-121 type prosite sequence SEHTVDKKKYAAELHLV description ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV source prosite : PS00162 143) 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 144) 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 145) chain A residue 165 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 146) chain A residue 172 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 147) chain B residue 165 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 148) chain B residue 172 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 149) 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 150) 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 151) 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 152) 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 153) chain A residue 198 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834 source Swiss-Prot : SWS_FT_FI4 154) chain B residue 198 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834 source Swiss-Prot : SWS_FT_FI4

Display surface Download Links