eF-site ID 5l3o-B PDB Code 5l3o Chain 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 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 307 source : AC7 2) chain B residue 96 type sequence H description binding site for residue ZN B 307 source : AC7 3) chain B residue 119 type sequence H description binding site for residue ZN B 307 source : AC7 4) chain B residue 7 type sequence Y description binding site for residue GOL B 312 source : AC8 5) chain B residue 62 type sequence N description binding site for residue GOL B 312 source : AC8 6) chain B residue 64 type sequence H description binding site for residue GOL B 312 source : AC8 7) chain B residue 65 type sequence A description binding site for residue GOL B 312 source : AC8 8) chain B residue 67 type sequence N description binding site for residue GOL B 312 source : AC8 9) chain B residue 92 type sequence Q description binding site for residue GOL B 312 source : AC8 10) chain B residue 94 type sequence H description binding site for residue GOL B 312 source : AC8 11) chain B residue 96 type sequence H description binding site for residue GOL B 312 source : AC8 12) chain B residue 199 type sequence T description binding site for residue GOL B 312 source : AC8 13) chain B residue 4 type sequence H description binding site for residue GOL B 313 source : AC9 14) chain B residue 11 type sequence N description binding site for residue GOL B 313 source : AC9 15) chain B residue 15 type sequence H description binding site for residue GOL B 313 source : AC9 16) chain B residue 16 type sequence W description binding site for residue GOL B 313 source : AC9 17) chain B residue 18 type sequence K description binding site for residue GOL B 313 source : AC9 18) chain B residue 19 type sequence D description binding site for residue GOL B 313 source : AC9 19) chain B residue 7 type sequence Y description binding site for residue GOL B 314 source : AD1 20) chain B residue 242 type sequence D description binding site for residue GOL B 314 source : AD1 21) chain B residue 244 type sequence W description binding site for residue GOL B 314 source : AD1 22) chain B residue 246 type sequence P description binding site for residue GOL B 314 source : AD1 23) chain B residue 163 type sequence L description binding site for residue GOL B 315 source : AD2 24) chain B residue 164 type sequence D description binding site for residue GOL B 315 source : AD2 25) chain B residue 167 type sequence K description binding site for residue GOL B 315 source : AD2 26) chain B residue 224 type sequence K description binding site for residue GOL B 315 source : AD2 27) chain B residue 227 type sequence K description binding site for residue GOL B 315 source : AD2 28) chain B residue 228 type sequence L description binding site for residue GOL B 315 source : AD2 29) chain B residue 131 type sequence G description binding site for residues 6H0 A 302 and QUJ A 312 source : AD3 30) chain B residue 129 type sequence D description binding site for residues QUK A 303 and QVS A 304 source : AD4 31) chain B residue 132 type sequence K description binding site for residues QUK A 303 and QVS A 304 source : AD4 32) chain B residue 131 type sequence G description binding site for residues QUK A 303 and QUJ A 312 source : AD5 33) chain B residue 129 type sequence D description binding site for residues QVS A 304 and QVE A 305 source : AD6 34) chain B residue 132 type sequence K description binding site for residues QVS A 304 and QVE A 305 source : AD6 35) chain B residue 3 type sequence H description binding site for residues QUJ A 310 and QUK B 301 source : AE1 36) chain B residue 19 type sequence D description binding site for residues QUJ A 310 and QUK B 301 source : AE1 37) chain B residue 20 type sequence F description binding site for residues QUJ A 310 and QUK B 301 source : AE1 38) chain B residue 2 type sequence S description binding site for residues QVS A 311 and QVE B 302 source : AE2 39) chain B residue 3 type sequence H description binding site for residues QVS A 311 and QVE B 302 source : AE2 40) chain B residue 2 type sequence S description binding site for residues QVS A 311 and QUK B 301 source : AE3 41) chain B residue 3 type sequence H description binding site for residues QVS A 311 and QUK B 301 source : AE3 42) chain B residue 94 type sequence H description binding site for residues QUJ B 303 and 6H0 B 308 source : AE7 43) chain B residue 96 type sequence H description binding site for residues QUJ B 303 and 6H0 B 308 source : AE7 44) chain B residue 119 type sequence H description binding site for residues QUJ B 303 and 6H0 B 308 source : AE7 45) chain B residue 130 type sequence F description binding site for residues QUJ B 303 and 6H0 B 308 source : AE7 46) chain B residue 197 type sequence L description binding site for residues QUJ B 303 and 6H0 B 308 source : AE7 47) chain B residue 198 type sequence T description binding site for residues QUJ B 303 and 6H0 B 308 source : AE7 48) chain B residue 199 type sequence T description binding site for residues QUJ B 303 and 6H0 B 308 source : AE7 49) chain B residue 201 type sequence P description binding site for residues QUJ B 303 and 6H0 B 308 source : AE7 50) chain B residue 208 type sequence W description binding site for residues QUJ B 303 and 6H0 B 308 source : AE7 51) chain B residue 3 type sequence H description binding site for residues QUJ B 303 and QUK B 309 source : AE8 52) chain B residue 135 type sequence Q description binding site for residues 6H0 B 304 and QUJ B 305 source : AE9 53) chain B residue 3 type sequence H description binding site for residues QUK B 309 and QVS B 310 source : AF1 54) chain B residue 19 type sequence D description binding site for residues QUK B 309 and QVS B 310 source : AF1 55) chain B residue 20 type sequence F description binding site for residues QUK B 309 and QVS B 310 source : AF1 56) chain B residue 2 type sequence S description binding site for residues QVS B 310 and QVE B 311 source : AF2 57) chain B residue 3 type sequence H description binding site for residues QVS B 310 and QVE B 311 source : AF2 58) chain B residue 19 type sequence D description binding site for residues QVS B 310 and QVE B 311 source : AF2 59) chain B residue 20 type sequence F description binding site for residues QVS B 310 and QVE B 311 source : AF2 60) chain B residue 64 type catalytic sequence H description 216 source MCSA : MCSA2 61) chain B residue 94 type catalytic sequence H description 216 source MCSA : MCSA2 62) chain B residue 96 type catalytic sequence H description 216 source MCSA : MCSA2 63) chain B residue 106 type catalytic sequence E description 216 source MCSA : MCSA2 64) chain B residue 119 type catalytic sequence H description 216 source MCSA : MCSA2 65) chain B residue 198 type catalytic sequence T description 216 source MCSA : MCSA2 66) 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 67) chain B residue 2 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P27139 source Swiss-Prot : SWS_FT_FI8 68) 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 69) 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 70) 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 71) 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 72) 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 73) chain B residue 165 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 74) chain B residue 172 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 75) 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 76) 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 77) chain B 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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