eF-site ID 5l9e-ABCD PDB Code 5l9e Chain A, B, C, D 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 C:  HWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPS LKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGP LDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHW NTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVL DSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLL ECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDN WRPAQPLKNRQIKASFK D:  HWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPS LKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGP LDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHW NTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVL DSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLL ECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDN WRPAQPLKNRQIKASF 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 307 source : AC2 5) chain A residue 64 type sequence H description binding site for residue ZN A 307 source : AC2 6) chain A residue 17 type sequence H description binding site for residue ZN A 308 source : AC3 7) chain C residue 26 type sequence E description binding site for residue ZN A 308 source : AC3 8) chain A residue 174 type sequence D description binding site for residue ZN A 309 source : AC4 9) chain A residue 34 type sequence D description binding site for residue ZN A 310 source : AC5 10) chain A residue 36 type sequence H description binding site for residue ZN A 310 source : AC5 11) chain A residue 186 type sequence E description binding site for residue ZN A 311 source : AC6 12) chain B residue 189 type sequence D description binding site for residue ZN A 311 source : AC6 13) chain A residue 52 type sequence D description binding site for residue ZN A 312 source : AC7 14) chain B residue 52 type sequence D description binding site for residue ZN A 312 source : AC7 15) chain A residue 15 type sequence H description binding site for residue ZN A 313 source : AC8 16) chain A residue 62 type sequence N description binding site for residue GOL A 314 source : AC9 17) chain A residue 65 type sequence A description binding site for residue GOL A 314 source : AC9 18) chain A residue 67 type sequence N description binding site for residue GOL A 314 source : AC9 19) chain A residue 92 type sequence Q description binding site for residue GOL A 314 source : AC9 20) chain A residue 189 type sequence D description binding site for residue ZN A 315 source : AD1 21) chain A residue 260 type sequence K description binding site for residue ZN A 315 source : AD1 22) chain B residue 186 type sequence E description binding site for residue ZN A 315 source : AD1 23) chain A residue 233 type sequence E description binding site for residue ZN A 316 source : AD2 24) chain A residue 233 type sequence E description binding site for residue ZN A 316 source : AD2 25) chain C residue 171 type sequence K description binding site for residue ZN A 316 source : AD2 26) chain C residue 233 type sequence E description binding site for residue ZN A 316 source : AD2 27) chain C residue 233 type sequence E description binding site for residue ZN A 316 source : AD2 28) chain B residue 94 type sequence H description binding site for residue ZN B 301 source : AD3 29) chain B residue 96 type sequence H description binding site for residue ZN B 301 source : AD3 30) chain B residue 119 type sequence H description binding site for residue ZN B 301 source : AD3 31) chain B residue 4 type sequence H description binding site for residue ZN B 307 source : AD4 32) chain B residue 64 type sequence H description binding site for residue ZN B 307 source : AD4 33) chain B residue 17 type sequence H description binding site for residue ZN B 308 source : AD5 34) chain B residue 18 type sequence K description binding site for residue ZN B 308 source : AD5 35) chain D residue 26 type sequence E description binding site for residue ZN B 308 source : AD5 36) chain B residue 174 type sequence D description binding site for residue ZN B 309 source : AD6 37) chain B residue 34 type sequence D description binding site for residue ZN B 310 source : AD7 38) chain B residue 36 type sequence H description binding site for residue ZN B 310 source : AD7 39) chain B residue 62 type sequence N description binding site for residue GOL B 311 source : AD8 40) chain B residue 65 type sequence A description binding site for residue GOL B 311 source : AD8 41) chain B residue 67 type sequence N description binding site for residue GOL B 311 source : AD8 42) chain B residue 92 type sequence Q description binding site for residue GOL B 311 source : AD8 43) chain C residue 94 type sequence H description binding site for residue ZN C 301 source : AD9 44) chain C residue 96 type sequence H description binding site for residue ZN C 301 source : AD9 45) chain C residue 119 type sequence H description binding site for residue ZN C 301 source : AD9 46) chain C residue 4 type sequence H description binding site for residue ZN C 307 source : AE1 47) chain C residue 64 type sequence H description binding site for residue ZN C 307 source : AE1 48) chain A residue 26 type sequence E description binding site for residue ZN C 308 source : AE2 49) chain C residue 17 type sequence H description binding site for residue ZN C 308 source : AE2 50) chain C residue 174 type sequence D description binding site for residue ZN C 309 source : AE3 51) chain B residue 14 type sequence E description binding site for residue ZN C 310 source : AE4 52) chain C residue 34 type sequence D description binding site for residue ZN C 310 source : AE4 53) chain C residue 36 type sequence H description binding site for residue ZN C 310 source : AE4 54) chain C residue 62 type sequence N description binding site for residue GOL C 311 source : AE5 55) chain C residue 67 type sequence N description binding site for residue GOL C 311 source : AE5 56) chain C residue 94 type sequence H description binding site for residue GOL C 311 source : AE5 57) chain C residue 199 type sequence T description binding site for residue GOL C 311 source : AE5 58) chain B residue 10 type sequence H description binding site for residue ZN C 312 source : AE6 59) chain C residue 36 type sequence H description binding site for residue ZN C 312 source : AE6 60) chain D residue 94 type sequence H description binding site for residue ZN D 301 source : AE7 61) chain D residue 96 type sequence H description binding site for residue ZN D 301 source : AE7 62) chain D residue 119 type sequence H description binding site for residue ZN D 301 source : AE7 63) chain D residue 4 type sequence H description binding site for residue ZN D 306 source : AE8 64) chain D residue 64 type sequence H description binding site for residue ZN D 306 source : AE8 65) chain B residue 26 type sequence E description binding site for residue ZN D 307 source : AE9 66) chain D residue 17 type sequence H description binding site for residue ZN D 307 source : AE9 67) chain D residue 174 type sequence D description binding site for residue ZN D 308 source : AF1 68) chain D residue 34 type sequence D description binding site for residue ZN D 309 source : AF2 69) chain D residue 36 type sequence H description binding site for residue ZN D 309 source : AF2 70) chain D residue 62 type sequence N description binding site for residue GOL D 310 source : AF3 71) chain D residue 65 type sequence A description binding site for residue GOL D 310 source : AF3 72) chain D residue 67 type sequence N description binding site for residue GOL D 310 source : AF3 73) chain D residue 92 type sequence Q description binding site for residue GOL D 310 source : AF3 74) chain B residue 233 type sequence E description binding site for residue ZN D 311 source : AF4 75) chain B residue 233 type sequence E description binding site for residue ZN D 311 source : AF4 76) chain D residue 233 type sequence E description binding site for residue ZN D 311 source : AF4 77) chain D residue 233 type sequence E description binding site for residue ZN D 311 source : AF4 78) chain A residue 94 type sequence H description binding site for residues 6H0 A 302 and QUJ A 303 source : AF5 79) chain A residue 96 type sequence H description binding site for residues 6H0 A 302 and QUJ A 303 source : AF5 80) chain A residue 119 type sequence H description binding site for residues 6H0 A 302 and QUJ A 303 source : AF5 81) chain A residue 130 type sequence F description binding site for residues 6H0 A 302 and QUJ A 303 source : AF5 82) chain A residue 197 type sequence L description binding site for residues 6H0 A 302 and QUJ A 303 source : AF5 83) chain A residue 198 type sequence T description binding site for residues 6H0 A 302 and QUJ A 303 source : AF5 84) chain A residue 199 type sequence T description binding site for residues 6H0 A 302 and QUJ A 303 source : AF5 85) chain A residue 208 type sequence W description binding site for residues 6H0 A 302 and QUJ A 303 source : AF5 86) chain A residue 4 type sequence H description binding site for residues QUJ A 303 and QVE A 304 source : AF6 87) chain A residue 169 type sequence K description binding site for residues QUJ A 303 and QVE A 304 source : AF6 88) chain A residue 4 type sequence H description binding site for residues QVE A 304 and QUJ A 305 source : AF7 89) chain A residue 19 type sequence D description binding site for residues QVE A 304 and QUJ A 305 source : AF7 90) chain A residue 20 type sequence F description binding site for residues QVE A 304 and QUJ A 305 source : AF7 91) chain A residue 169 type sequence K description binding site for residues QVE A 304 and QUJ A 305 source : AF7 92) chain A residue 201 type sequence P description binding site for residues QVE A 304 and QUJ A 305 source : AF7 93) chain A residue 4 type sequence H description binding site for residues QUJ A 305 and QVE A 306 source : AF8 94) chain A residue 5 type sequence W description binding site for residues QUJ A 305 and QVE A 306 source : AF8 95) chain A residue 19 type sequence D description binding site for residues QUJ A 305 and QVE A 306 source : AF8 96) chain A residue 20 type sequence F description binding site for residues QUJ A 305 and QVE A 306 source : AF8 97) chain A residue 64 type sequence H description binding site for residues QUJ A 305 and QVE A 306 source : AF8 98) chain A residue 201 type sequence P description binding site for residues QUJ A 305 and QVE A 306 source : AF8 99) chain B residue 94 type sequence H description binding site for residues 6H0 B 302 and QUJ B 303 source : AF9 100) chain B residue 96 type sequence H description binding site for residues 6H0 B 302 and QUJ B 303 source : AF9 101) chain B residue 119 type sequence H description binding site for residues 6H0 B 302 and QUJ B 303 source : AF9 102) chain B residue 130 type sequence F description binding site for residues 6H0 B 302 and QUJ B 303 source : AF9 103) chain B residue 197 type sequence L description binding site for residues 6H0 B 302 and QUJ B 303 source : AF9 104) chain B residue 198 type sequence T description binding site for residues 6H0 B 302 and QUJ B 303 source : AF9 105) chain B residue 199 type sequence T description binding site for residues 6H0 B 302 and QUJ B 303 source : AF9 106) chain B residue 208 type sequence W description binding site for residues 6H0 B 302 and QUJ B 303 source : AF9 107) chain B residue 4 type sequence H description binding site for residues QUJ B 303 and QVE B 304 source : AG1 108) chain B residue 4 type sequence H description binding site for residues QVE B 304 and QUJ B 305 source : AG2 109) chain B residue 19 type sequence D description binding site for residues QVE B 304 and QUJ B 305 source : AG2 110) chain B residue 20 type sequence F description binding site for residues QVE B 304 and QUJ B 305 source : AG2 111) chain B residue 4 type sequence H description binding site for residues QUJ B 305 and QVE B 306 source : AG3 112) chain B residue 5 type sequence W description binding site for residues QUJ B 305 and QVE B 306 source : AG3 113) chain B residue 19 type sequence D description binding site for residues QUJ B 305 and QVE B 306 source : AG3 114) chain B residue 20 type sequence F description binding site for residues QUJ B 305 and QVE B 306 source : AG3 115) chain B residue 64 type sequence H description binding site for residues QUJ B 305 and QVE B 306 source : AG3 116) chain B residue 201 type sequence P description binding site for residues QUJ B 305 and QVE B 306 source : AG3 117) chain B residue 4 type sequence H description binding site for residues QUJ B 312 and QVE D 304 source : AG4 118) chain D residue 4 type sequence H description binding site for residues QUJ B 312 and QVE D 304 source : AG4 119) chain D residue 19 type sequence D description binding site for residues QUJ B 312 and QVE D 304 source : AG4 120) chain D residue 20 type sequence F description binding site for residues QUJ B 312 and QVE D 304 source : AG4 121) chain D residue 169 type sequence K description binding site for residues QUJ B 312 and QVE D 304 source : AG4 122) chain B residue 19 type sequence D description binding site for residues QUJ B 312 and QVE D 305 source : AG5 123) chain B residue 20 type sequence F description binding site for residues QUJ B 312 and QVE D 305 source : AG5 124) chain D residue 4 type sequence H description binding site for residues QUJ B 312 and QVE D 305 source : AG5 125) chain D residue 5 type sequence W description binding site for residues QUJ B 312 and QVE D 305 source : AG5 126) chain D residue 19 type sequence D description binding site for residues QUJ B 312 and QVE D 305 source : AG5 127) chain D residue 20 type sequence F description binding site for residues QUJ B 312 and QVE D 305 source : AG5 128) chain D residue 64 type sequence H description binding site for residues QUJ B 312 and QVE D 305 source : AG5 129) chain C residue 92 type sequence Q description binding site for residues 6H0 C 302 and QUJ C 303 source : AG6 130) chain C residue 94 type sequence H description binding site for residues 6H0 C 302 and QUJ C 303 source : AG6 131) chain C residue 96 type sequence H description binding site for residues 6H0 C 302 and QUJ C 303 source : AG6 132) chain C residue 119 type sequence H description binding site for residues 6H0 C 302 and QUJ C 303 source : AG6 133) chain C residue 130 type sequence F description binding site for residues 6H0 C 302 and QUJ C 303 source : AG6 134) chain C residue 197 type sequence L description binding site for residues 6H0 C 302 and QUJ C 303 source : AG6 135) chain C residue 198 type sequence T description binding site for residues 6H0 C 302 and QUJ C 303 source : AG6 136) chain C residue 199 type sequence T description binding site for residues 6H0 C 302 and QUJ C 303 source : AG6 137) chain C residue 208 type sequence W description binding site for residues 6H0 C 302 and QUJ C 303 source : AG6 138) chain C residue 4 type sequence H description binding site for residues QUJ C 303 and QVE C 304 source : AG7 139) chain C residue 169 type sequence K description binding site for residues QUJ C 303 and QVE C 304 source : AG7 140) chain C residue 4 type sequence H description binding site for residues QVE C 304 and QUJ C 305 source : AG8 141) chain C residue 19 type sequence D description binding site for residues QVE C 304 and QUJ C 305 source : AG8 142) chain C residue 20 type sequence F description binding site for residues QVE C 304 and QUJ C 305 source : AG8 143) chain C residue 169 type sequence K description binding site for residues QVE C 304 and QUJ C 305 source : AG8 144) chain C residue 4 type sequence H description binding site for residues QUJ C 305 and QVE C 306 source : AG9 145) chain C residue 5 type sequence W description binding site for residues QUJ C 305 and QVE C 306 source : AG9 146) chain C residue 19 type sequence D description binding site for residues QUJ C 305 and QVE C 306 source : AG9 147) chain C residue 20 type sequence F description binding site for residues QUJ C 305 and QVE C 306 source : AG9 148) chain C residue 64 type sequence H description binding site for residues QUJ C 305 and QVE C 306 source : AG9 149) chain D residue 92 type sequence Q description binding site for residues 6H0 D 302 and QUJ D 303 source : AH1 150) chain D residue 94 type sequence H description binding site for residues 6H0 D 302 and QUJ D 303 source : AH1 151) chain D residue 96 type sequence H description binding site for residues 6H0 D 302 and QUJ D 303 source : AH1 152) chain D residue 119 type sequence H description binding site for residues 6H0 D 302 and QUJ D 303 source : AH1 153) chain D residue 130 type sequence F description binding site for residues 6H0 D 302 and QUJ D 303 source : AH1 154) chain D residue 197 type sequence L description binding site for residues 6H0 D 302 and QUJ D 303 source : AH1 155) chain D residue 198 type sequence T description binding site for residues 6H0 D 302 and QUJ D 303 source : AH1 156) chain D residue 199 type sequence T description binding site for residues 6H0 D 302 and QUJ D 303 source : AH1 157) chain D residue 208 type sequence W description binding site for residues 6H0 D 302 and QUJ D 303 source : AH1 158) chain D residue 4 type sequence H description binding site for residues QUJ D 303 and QVE D 304 source : AH2 159) chain D residue 169 type sequence K description binding site for residues QUJ D 303 and QVE D 304 source : AH2 160) chain A residue 64 type catalytic sequence H description 216 source MCSA : MCSA1 161) chain A residue 94 type catalytic sequence H description 216 source MCSA : MCSA1 162) chain A residue 96 type catalytic sequence H description 216 source MCSA : MCSA1 163) chain A residue 106 type catalytic sequence E description 216 source MCSA : MCSA1 164) chain A residue 119 type catalytic sequence H description 216 source MCSA : MCSA1 165) chain A residue 198 type catalytic sequence T description 216 source MCSA : MCSA1 166) chain B residue 64 type catalytic sequence H description 216 source MCSA : MCSA2 167) chain B residue 94 type catalytic sequence H description 216 source MCSA : MCSA2 168) chain B residue 96 type catalytic sequence H description 216 source MCSA : MCSA2 169) chain B residue 106 type catalytic sequence E description 216 source MCSA : MCSA2 170) chain B residue 119 type catalytic sequence H description 216 source MCSA : MCSA2 171) chain B residue 198 type catalytic sequence T description 216 source MCSA : MCSA2 172) chain C residue 64 type catalytic sequence H description 216 source MCSA : MCSA3 173) chain C residue 94 type catalytic sequence H description 216 source MCSA : MCSA3 174) chain C residue 96 type catalytic sequence H description 216 source MCSA : MCSA3 175) chain C residue 106 type catalytic sequence E description 216 source MCSA : MCSA3 176) chain C residue 119 type catalytic sequence H description 216 source MCSA : MCSA3 177) chain C residue 198 type catalytic sequence T description 216 source MCSA : MCSA3 178) chain D residue 64 type catalytic sequence H description 216 source MCSA : MCSA4 179) chain D residue 94 type catalytic sequence H description 216 source MCSA : MCSA4 180) chain D residue 96 type catalytic sequence H description 216 source MCSA : MCSA4 181) chain D residue 106 type catalytic sequence E description 216 source MCSA : MCSA4 182) chain D residue 119 type catalytic sequence H description 216 source MCSA : MCSA4 183) chain D residue 198 type catalytic sequence T description 216 source MCSA : MCSA4 184) chain A residue 105-121 type prosite sequence SEHTVDKKKYAAELHLV description ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV source prosite : PS00162 185) 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 186) 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 187) chain C 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 188) chain D 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 189) 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 190) 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 191) chain C 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 192) chain D 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 193) chain A residue 2 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P27139 source Swiss-Prot : SWS_FT_FI8 194) chain B residue 2 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P27139 source Swiss-Prot : SWS_FT_FI8 195) chain A residue 165 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 196) chain A residue 172 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 197) chain B residue 165 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 198) chain B residue 172 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 199) chain C residue 165 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 200) chain C residue 172 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 201) chain D residue 165 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 202) chain D residue 172 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 203) 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 204) 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 205) chain C 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 206) chain D 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 207) 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 208) 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 209) 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 210) 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 211) chain C 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 212) chain C 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 213) chain D 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 214) chain D 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 215) chain A residue 198 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834 source Swiss-Prot : SWS_FT_FI4 216) chain B residue 198 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834 source Swiss-Prot : SWS_FT_FI4 217) chain C residue 198 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834 source Swiss-Prot : SWS_FT_FI4 218) chain D residue 198 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834 source Swiss-Prot : SWS_FT_FI4 219) 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 220) 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 221) chain C 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 222) chain D 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 223) 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 224) 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 225) 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 226) 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 227) chain C 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 228) chain C 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 229) chain D 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 230) chain D 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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