eF-site ID 5wg7-A PDB Code 5wg7 Chain A click to enlarge Title Human Carbonic Anhydrase II complexed with AceK Classification LYASE Compound Carbonic anhydrase 2 Source Homo sapiens (Human) (CAH2_HUMAN) Sequence A:  HWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPS LKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGP LDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHW NTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVL DSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLL ECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDN WRPAQPLKNRQIKASFK Description Functional site 1) chain A residue 92 type sequence Q description binding site for residue AUD A 301 source : AC1 2) chain A residue 94 type sequence H description binding site for residue AUD A 301 source : AC1 3) chain A residue 119 type sequence H description binding site for residue AUD A 301 source : AC1 4) chain A residue 121 type sequence V description binding site for residue AUD A 301 source : AC1 5) chain A residue 143 type sequence V description binding site for residue AUD A 301 source : AC1 6) chain A residue 198 type sequence L description binding site for residue AUD A 301 source : AC1 7) chain A residue 199 type sequence T description binding site for residue AUD A 301 source : AC1 8) chain A residue 200 type sequence T description binding site for residue AUD A 301 source : AC1 9) chain A residue 164 type sequence L description binding site for residue AUD A 302 source : AC2 10) chain A residue 165 type sequence D description binding site for residue AUD A 302 source : AC2 11) chain A residue 228 type sequence K description binding site for residue AUD A 302 source : AC2 12) chain A residue 229 type sequence L description binding site for residue AUD A 302 source : AC2 13) chain A residue 225 type sequence K description binding site for residue AUD A 303 source : AC3 14) chain A residue 102 type sequence G description binding site for residue AUD A 304 source : AC4 15) chain A residue 111 type sequence K description binding site for residue AUD A 304 source : AC4 16) chain A residue 112 type sequence K description binding site for residue AUD A 304 source : AC4 17) chain A residue 113 type sequence K description binding site for residue AUD A 304 source : AC4 18) chain A residue 128 type sequence Y description binding site for residue AUD A 304 source : AC4 19) chain A residue 133 type sequence K description binding site for residue AUD A 304 source : AC4 20) chain A residue 6 type sequence G description binding site for residue AUD A 305 source : AC5 21) chain A residue 7 type sequence Y description binding site for residue AUD A 305 source : AC5 22) chain A residue 8 type sequence G description binding site for residue AUD A 305 source : AC5 23) chain A residue 10 type sequence H description binding site for residue AUD A 305 source : AC5 24) chain A residue 231 type sequence F description binding site for residue AUD A 305 source : AC5 25) chain A residue 239 type sequence E description binding site for residue AUD A 305 source : AC5 26) chain A residue 131 type sequence F description binding site for residue AUD A 306 source : AC6 27) chain A residue 202 type sequence P description binding site for residue AUD A 306 source : AC6 28) chain A residue 94 type sequence H description binding site for residue ZN A 307 source : AC7 29) chain A residue 96 type sequence H description binding site for residue ZN A 307 source : AC7 30) chain A residue 119 type sequence H description binding site for residue ZN A 307 source : AC7 31) chain A residue 62 type sequence N description binding site for residue GOL A 308 source : AC8 32) chain A residue 64 type sequence H description binding site for residue GOL A 308 source : AC8 33) chain A residue 65 type sequence A description binding site for residue GOL A 308 source : AC8 34) chain A residue 67 type sequence N description binding site for residue GOL A 308 source : AC8 35) chain A residue 92 type sequence Q description binding site for residue GOL A 308 source : AC8 36) chain A residue 200 type sequence T description binding site for residue GOL A 308 source : AC8 37) chain A residue 7 type sequence Y description binding site for residue GOL A 309 source : AC9 38) chain A residue 243 type sequence D description binding site for residue GOL A 309 source : AC9 39) chain A residue 245 type sequence W description binding site for residue GOL A 309 source : AC9 40) chain A residue 247 type sequence P description binding site for residue GOL A 309 source : AC9 41) chain A residue 235 type sequence G description binding site for residue GOL A 310 source : AD1 42) 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 43) 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 44) chain A residue 64 type catalytic sequence H description 216 source MCSA : MCSA1 45) chain A residue 94 type catalytic sequence H description 216 source MCSA : MCSA1 46) chain A residue 96 type catalytic sequence H description 216 source MCSA : MCSA1 47) chain A residue 106 type catalytic sequence E description 216 source MCSA : MCSA1 48) chain A residue 119 type catalytic sequence H description 216 source MCSA : MCSA1 49) chain A residue 199 type catalytic sequence T description 216 source MCSA : MCSA1 50) 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 51) 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 52) chain A residue 199 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834 source Swiss-Prot : SWS_FT_FI4 53) chain A residue 105-121 type prosite sequence SEHTVDKKKYAAELHLV description ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV source prosite : PS00162 54) 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 55) 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 56) 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 57) 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 58) chain A residue 166 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 59) chain A residue 173 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8

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