eF-site ID 5l70-B PDB Code 5l70 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 (5L70) Sequence B:  HHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDP SLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGG PLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVH WNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDV LDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPL LECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVD NWRPAQPLKNRQIKASFK Description Functional site 1) chain B residue 34 type sequence D description binding site for residue ZN A 305 source : AC5 2) chain B residue 36 type sequence H description binding site for residue ZN A 306 source : AC6 3) chain B residue 233 type sequence E description binding site for residue ZN A 307 source : AC7 4) chain B residue 94 type sequence H description binding site for residue ZN B 301 source : AD3 5) chain B residue 96 type sequence H description binding site for residue ZN B 301 source : AD3 6) chain B residue 119 type sequence H description binding site for residue ZN B 301 source : AD3 7) chain B residue 4 type sequence H description binding site for residue ZN B 302 source : AD4 8) chain B residue 64 type sequence H description binding site for residue ZN B 302 source : AD4 9) chain B residue 5 type sequence W description binding site for residue GOL B 303 source : AD5 10) chain B residue 62 type sequence N description binding site for residue GOL B 303 source : AD5 11) chain B residue 199 type sequence T description binding site for residue GOL B 303 source : AD5 12) chain B residue 200 type sequence P description binding site for residue GOL B 303 source : AD5 13) chain B residue 201 type sequence P description binding site for residue GOL B 303 source : AD5 14) chain B residue 17 type sequence H description binding site for residue ZN B 304 source : AD6 15) chain B residue 72 type sequence D description binding site for residue ZN B 305 source : AD7 16) chain B residue 35 type sequence T description binding site for residue GOL B 306 source : AD8 17) chain B residue 38 type sequence A description binding site for residue GOL B 306 source : AD8 18) chain B residue 191 type sequence W description binding site for residue GOL B 306 source : AD8 19) chain B residue 259 type sequence F description binding site for residue GOL B 306 source : AD8 20) chain B residue 260 type sequence K description binding site for residue GOL B 306 source : AD8 21) chain B residue 5 type sequence W description binding site for residues QVS A 305 and QOL B 301 source : AE2 22) chain B residue 62 type sequence N description binding site for residues QVS A 305 and QOL B 301 source : AE2 23) chain B residue 199 type sequence T description binding site for residues QVS A 305 and QOL B 301 source : AE2 24) chain B residue 200 type sequence P description binding site for residues QVS A 305 and QOL B 301 source : AE2 25) chain B residue 201 type sequence P description binding site for residues QVS A 305 and QOL B 301 source : AE2 26) chain B residue 4 type sequence H description binding site for residues QOL A 316 and QVS A 317 source : AE4 27) chain B residue 4 type sequence H description binding site for residues QVS A 317 and QUK A 318 source : AE5 28) chain B residue 19 type sequence D description binding site for residues QVS A 317 and QUK A 318 source : AE5 29) chain B residue 20 type sequence F description binding site for residues QVS A 317 and QUK A 318 source : AE5 30) chain B residue 4 type sequence H description binding site for residues QUK A 318 and QVE A 319 source : AE6 31) chain B residue 5 type sequence W description binding site for residues QUK A 318 and QVE A 319 source : AE6 32) chain B residue 19 type sequence D description binding site for residues QUK A 318 and QVE A 319 source : AE6 33) chain B residue 20 type sequence F description binding site for residues QUK A 318 and QVE A 319 source : AE6 34) chain B residue 64 type sequence H description binding site for residues QUK A 318 and QVE A 319 source : AE6 35) chain B residue 94 type sequence H description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 36) chain B residue 96 type sequence H description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 37) chain B residue 119 type sequence H description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 38) chain B residue 121 type sequence V description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 39) chain B residue 130 type sequence F description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 40) chain B residue 142 type sequence V description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 41) chain B residue 197 type sequence L description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 42) chain B residue 198 type sequence T description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 43) chain B residue 199 type sequence T description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 44) chain B residue 201 type sequence P description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 45) chain B residue 208 type sequence W description binding site for residues QOL B 301 and 6H0 B 303 source : AE7 46) chain B residue 64 type catalytic sequence H description 216 source MCSA : MCSA2 47) chain B residue 94 type catalytic sequence H description 216 source MCSA : MCSA2 48) chain B residue 96 type catalytic sequence H description 216 source MCSA : MCSA2 49) chain B residue 106 type catalytic sequence E description 216 source MCSA : MCSA2 50) chain B residue 119 type catalytic sequence H description 216 source MCSA : MCSA2 51) chain B residue 198 type catalytic sequence T description 216 source MCSA : MCSA2 52) 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 53) 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 54) 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 55) 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 56) chain B residue 198 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834 source Swiss-Prot : SWS_FT_FI4 57) 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 58) 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 59) 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 60) 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 61) chain B residue 165 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 62) chain B residue 172 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9

Display surface Download Links