eF-site ID 5l70-AB PDB Code 5l70 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:  HHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDP SLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGG PLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVH WNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDV LDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPL LECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVD NWRPAQPLKNRQIKASFK B:  HHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDP SLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGG PLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVH WNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDV LDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPL LECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVD NWRPAQPLKNRQIKASFK 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 4 type sequence H description binding site for residue ZN A 303 source : AC2 5) chain A residue 64 type sequence H description binding site for residue ZN A 303 source : AC2 6) chain A residue 5 type sequence W description binding site for residue GOL A 304 source : AC3 7) chain A residue 62 type sequence N description binding site for residue GOL A 304 source : AC3 8) chain A residue 64 type sequence H description binding site for residue GOL A 304 source : AC3 9) chain A residue 199 type sequence T description binding site for residue GOL A 304 source : AC3 10) chain A residue 200 type sequence P description binding site for residue GOL A 304 source : AC3 11) chain A residue 17 type sequence H description binding site for residue ZN A 308 source : AC4 12) chain A residue 36 type sequence H description binding site for residue ZN A 309 source : AC5 13) chain B residue 34 type sequence D description binding site for residue ZN A 309 source : AC5 14) chain A residue 34 type sequence D description binding site for residue ZN A 310 source : AC6 15) chain B residue 36 type sequence H description binding site for residue ZN A 310 source : AC6 16) chain A residue 174 type sequence D description binding site for residue ZN A 311 source : AC7 17) chain B residue 233 type sequence E description binding site for residue ZN A 311 source : AC7 18) chain A residue 238 type sequence E description binding site for residue ZN A 312 source : AC8 19) chain A residue 72 type sequence D description binding site for residue ZN A 314 source : AD1 20) chain A residue 35 type sequence T description binding site for residue GOL A 315 source : AD2 21) chain A residue 38 type sequence A description binding site for residue GOL A 315 source : AD2 22) chain A residue 191 type sequence W description binding site for residue GOL A 315 source : AD2 23) chain A residue 259 type sequence F description binding site for residue GOL A 315 source : AD2 24) chain A residue 260 type sequence K description binding site for residue GOL A 315 source : AD2 25) chain B residue 94 type sequence H description binding site for residue ZN B 302 source : AD3 26) chain B residue 96 type sequence H description binding site for residue ZN B 302 source : AD3 27) chain B residue 119 type sequence H description binding site for residue ZN B 302 source : AD3 28) chain B residue 4 type sequence H description binding site for residue ZN B 304 source : AD4 29) chain B residue 64 type sequence H description binding site for residue ZN B 304 source : AD4 30) chain B residue 5 type sequence W description binding site for residue GOL B 305 source : AD5 31) chain B residue 62 type sequence N description binding site for residue GOL B 305 source : AD5 32) chain B residue 199 type sequence T description binding site for residue GOL B 305 source : AD5 33) chain B residue 200 type sequence P description binding site for residue GOL B 305 source : AD5 34) chain B residue 201 type sequence P description binding site for residue GOL B 305 source : AD5 35) chain B residue 17 type sequence H description binding site for residue ZN B 306 source : AD6 36) chain B residue 72 type sequence D description binding site for residue ZN B 307 source : AD7 37) chain B residue 35 type sequence T description binding site for residue GOL B 308 source : AD8 38) chain B residue 38 type sequence A description binding site for residue GOL B 308 source : AD8 39) chain B residue 191 type sequence W description binding site for residue GOL B 308 source : AD8 40) chain B residue 259 type sequence F description binding site for residue GOL B 308 source : AD8 41) chain B residue 260 type sequence K description binding site for residue GOL B 308 source : AD8 42) chain A residue 94 type sequence H description binding site for residues 6H0 A 302 and QOL A 316 source : AD9 43) chain A residue 96 type sequence H description binding site for residues 6H0 A 302 and QOL A 316 source : AD9 44) chain A residue 119 type sequence H description binding site for residues 6H0 A 302 and QOL A 316 source : AD9 45) chain A residue 121 type sequence V description binding site for residues 6H0 A 302 and QOL A 316 source : AD9 46) chain A residue 130 type sequence F description binding site for residues 6H0 A 302 and QOL A 316 source : AD9 47) chain A residue 142 type sequence V description binding site for residues 6H0 A 302 and QOL A 316 source : AD9 48) chain A residue 197 type sequence L description binding site for residues 6H0 A 302 and QOL A 316 source : AD9 49) chain A residue 198 type sequence T description binding site for residues 6H0 A 302 and QOL A 316 source : AD9 50) chain A residue 199 type sequence T description binding site for residues 6H0 A 302 and QOL A 316 source : AD9 51) chain A residue 208 type sequence W description binding site for residues 6H0 A 302 and QOL A 316 source : AD9 52) chain A residue 4 type sequence H description binding site for residues QVS A 305 and QUK A 306 source : AE1 53) chain A residue 19 type sequence D description binding site for residues QVS A 305 and QUK A 306 source : AE1 54) chain A residue 20 type sequence F description binding site for residues QVS A 305 and QUK A 306 source : AE1 55) chain A residue 4 type sequence H description binding site for residues QVS A 305 and QOL B 301 source : AE2 56) chain A residue 94 type sequence H description binding site for residues QVS A 305 and QOL B 301 source : AE2 57) chain A residue 96 type sequence H description binding site for residues QVS A 305 and QOL B 301 source : AE2 58) chain A residue 119 type sequence H description binding site for residues QVS A 305 and QOL B 301 source : AE2 59) chain B residue 5 type sequence W description binding site for residues QVS A 305 and QOL B 301 source : AE2 60) chain B residue 62 type sequence N description binding site for residues QVS A 305 and QOL B 301 source : AE2 61) chain B residue 199 type sequence T description binding site for residues QVS A 305 and QOL B 301 source : AE2 62) chain B residue 200 type sequence P description binding site for residues QVS A 305 and QOL B 301 source : AE2 63) chain B residue 201 type sequence P description binding site for residues QVS A 305 and QOL B 301 source : AE2 64) chain A residue 4 type sequence H description binding site for residues QUK A 306 and QVE A 307 source : AE3 65) chain A residue 5 type sequence W description binding site for residues QUK A 306 and QVE A 307 source : AE3 66) chain A residue 19 type sequence D description binding site for residues QUK A 306 and QVE A 307 source : AE3 67) chain A residue 20 type sequence F description binding site for residues QUK A 306 and QVE A 307 source : AE3 68) chain A residue 64 type sequence H description binding site for residues QUK A 306 and QVE A 307 source : AE3 69) chain B residue 4 type sequence H description binding site for residues QOL A 316 and QVS A 317 source : AE4 70) chain B residue 4 type sequence H description binding site for residues QVS A 317 and QUK A 318 source : AE5 71) chain B residue 19 type sequence D description binding site for residues QVS A 317 and QUK A 318 source : AE5 72) chain B residue 20 type sequence F description binding site for residues QVS A 317 and QUK A 318 source : AE5 73) chain B residue 4 type sequence H description binding site for residues QUK A 318 and QVE A 319 source : AE6 74) chain B residue 5 type sequence W description binding site for residues QUK A 318 and QVE A 319 source : AE6 75) chain B residue 19 type sequence D description binding site for residues QUK A 318 and QVE A 319 source : AE6 76) chain B residue 20 type sequence F description binding site for residues QUK A 318 and QVE A 319 source : AE6 77) chain B residue 64 type sequence H description binding site for residues QUK A 318 and QVE A 319 source : AE6 78) chain B residue 94 type sequence H description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 79) chain B residue 96 type sequence H description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 80) chain B residue 119 type sequence H description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 81) chain B residue 121 type sequence V description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 82) chain B residue 130 type sequence F description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 83) chain B residue 142 type sequence V description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 84) chain B residue 197 type sequence L description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 85) chain B residue 198 type sequence T description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 86) chain B residue 199 type sequence T description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 87) chain B residue 201 type sequence P description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 88) chain B residue 208 type sequence W description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 89) chain A residue 64 type catalytic sequence H description 216 source MCSA : MCSA1 90) chain A residue 94 type catalytic sequence H description 216 source MCSA : MCSA1 91) chain A residue 96 type catalytic sequence H description 216 source MCSA : MCSA1 92) chain A residue 106 type catalytic sequence E description 216 source MCSA : MCSA1 93) chain A residue 119 type catalytic sequence H description 216 source MCSA : MCSA1 94) chain A residue 198 type catalytic sequence T description 216 source MCSA : MCSA1 95) chain B residue 64 type catalytic sequence H description 216 source MCSA : MCSA2 96) chain B residue 94 type catalytic sequence H description 216 source MCSA : MCSA2 97) chain B residue 96 type catalytic sequence H description 216 source MCSA : MCSA2 98) chain B residue 106 type catalytic sequence E description 216 source MCSA : MCSA2 99) chain B residue 119 type catalytic sequence H description 216 source MCSA : MCSA2 100) chain B residue 198 type catalytic sequence T description 216 source MCSA : MCSA2 101) 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 102) 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 103) chain A residue 198 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834 source Swiss-Prot : SWS_FT_FI4 104) chain B residue 198 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834 source Swiss-Prot : SWS_FT_FI4 105) 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 106) 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 107) 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 108) 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 109) chain A residue 105-121 type prosite sequence SEHTVDKKKYAAELHLV description ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV source prosite : PS00162 110) chain A residue 165 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 111) chain A residue 172 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 112) chain B residue 165 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 113) chain B residue 172 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 114) 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 115) 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 116) 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 117) 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 118) 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 119) 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 120) 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 121) 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 122) 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 123) 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

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