eF-site ID 1bxs-ABCD PDB Code 1bxs Chain A, B, C, D click to enlarge Title SHEEP LIVER CLASS 1 ALDEHYDE DEHYDROGENASE WITH NAD BOUND Classification OXIDOREDUCTASE Compound ALDEHYDE DEHYDROGENASE Source ORGANISM_COMMON: sheep; ORGANISM_SCIENTIFIC: Ovis aries; Sequence A:  DVPAPLTNLQFKYTKIFINNEWHSSVSGKKFPVFNPATEE KLCEVEEGDKEDVDKAVKAARQAFQIGSPWRTMDASERGR LLNKLADLIERDRLLLATMEAMNGGKLFSNAYLMDLGGCI KTLRYCAGWADKIQGRTIPMDGNFFTYTRSEPVGVCGQII PWNFPLLMFLWKIGPALSCGNTVVVKPAEQTPLTALHMGS LIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGS TEVGKLIKEAAGKSNLKRVSLELGGKSPCIVFADADLDNA VEFAHQGVFYHQGQCCIAASRLFVEESIYDEFVRRSVERA KKYVLGNPLTPGVSQGPQIDKEQYEKILDLIESGKKEGAK LECGGGPWGNKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQ IMKFKSLDDVIKRANNTFYGLSAGIFTNDIDKAITVSSAL QSGTVWVNCYSVVSAQCPFGGFKMSGNGRELGEYGFHEYT EVKTVTIKISQKNS B:  DVPAPLTNLQFKYTKIFINNEWHSSVSGKKFPVFNPATEE KLCEVEEGDKEDVDKAVKAARQAFQIGSPWRTMDASERGR LLNKLADLIERDRLLLATMEAMNGGKLFSNAYLMDLGGCI KTLRYCAGWADKIQGRTIPMDGNFFTYTRSEPVGVCGQII PWNFPLLMFLWKIGPALSCGNTVVVKPAEQTPLTALHMGS LIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGS TEVGKLIKEAAGKSNLKRVSLELGGKSPCIVFADADLDNA VEFAHQGVFYHQGQCCIAASRLFVEESIYDEFVRRSVERA KKYVLGNPLTPGVSQGPQIDKEQYEKILDLIESGKKEGAK LECGGGPWGNKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQ IMKFKSLDDVIKRANNTFYGLSAGIFTNDIDKAITVSSAL QSGTVWVNCYSVVSAQCPFGGFKMSGNGRELGEYGFHEYT EVKTVTIKISQKNS C:  DVPAPLTNLQFKYTKIFINNEWHSSVSGKKFPVFNPATEE KLCEVEEGDKEDVDKAVKAARQAFQIGSPWRTMDASERGR LLNKLADLIERDRLLLATMEAMNGGKLFSNAYLMDLGGCI KTLRYCAGWADKIQGRTIPMDGNFFTYTRSEPVGVCGQII PWNFPLLMFLWKIGPALSCGNTVVVKPAEQTPLTALHMGS LIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGS TEVGKLIKEAAGKSNLKRVSLELGGKSPCIVFADADLDNA VEFAHQGVFYHQGQCCIAASRLFVEESIYDEFVRRSVERA KKYVLGNPLTPGVSQGPQIDKEQYEKILDLIESGKKEGAK LECGGGPWGNKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQ IMKFKSLDDVIKRANNTFYGLSAGIFTNDIDKAITVSSAL QSGTVWVNCYSVVSAQCPFGGFKMSGNGRELGEYGFHEYT EVKTVTIKISQKNS D:  DVPAPLTNLQFKYTKIFINNEWHSSVSGKKFPVFNPATEE KLCEVEEGDKEDVDKAVKAARQAFQIGSPWRTMDASERGR LLNKLADLIERDRLLLATMEAMNGGKLFSNAYLMDLGGCI KTLRYCAGWADKIQGRTIPMDGNFFTYTRSEPVGVCGQII PWNFPLLMFLWKIGPALSCGNTVVVKPAEQTPLTALHMGS LIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGS TEVGKLIKEAAGKSNLKRVSLELGGKSPCIVFADADLDNA VEFAHQGVFYHQGQCCIAASRLFVEESIYDEFVRRSVERA KKYVLGNPLTPGVSQGPQIDKEQYEKILDLIESGKKEGAK LECGGGPWGNKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQ IMKFKSLDDVIKRANNTFYGLSAGIFTNDIDKAITVSSAL QSGTVWVNCYSVVSAQCPFGGFKMSGNGRELGEYGFHEYT EVKTVTIKISQKNS Description Functional site 1) chain A residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 2) chain A residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 3) chain A residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 4) chain A residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 5) chain A residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 6) chain A residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 7) chain A residue 194 type sequence A description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 8) chain A residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 9) chain A residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 10) chain A residue 226 type sequence P description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 11) chain A residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 12) chain A residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 13) chain A residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 14) chain A residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 15) chain A residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 16) chain A residue 249 type sequence V description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 17) chain A residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 18) chain A residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 19) chain A residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 20) chain A residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 21) chain A residue 349 type sequence Q description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 22) chain A residue 352 type sequence K description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 23) chain A residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 24) chain A residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD A 550 source : AC1 25) chain B residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 26) chain B residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 27) chain B residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 28) chain B residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 29) chain B residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 30) chain B residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 31) chain B residue 194 type sequence A description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 32) chain B residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 33) chain B residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 34) chain B residue 226 type sequence P description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 35) chain B residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 36) chain B residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 37) chain B residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 38) chain B residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 39) chain B residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 40) chain B residue 249 type sequence V description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 41) chain B residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 42) chain B residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 43) chain B residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 44) chain B residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 45) chain B residue 349 type sequence Q description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 46) chain B residue 352 type sequence K description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 47) chain B residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 48) chain B residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD B 550 source : AC2 49) chain C residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 50) chain C residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 51) chain C residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 52) chain C residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 53) chain C residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 54) chain C residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 55) chain C residue 194 type sequence A description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 56) chain C residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 57) chain C residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 58) chain C residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 59) chain C residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 60) chain C residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 61) chain C residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 62) chain C residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 63) chain C residue 249 type sequence V description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 64) chain C residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 65) chain C residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 66) chain C residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 67) chain C residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 68) chain C residue 349 type sequence Q description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 69) chain C residue 352 type sequence K description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 70) chain C residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 71) chain C residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 72) chain D residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 73) chain D residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 74) chain D residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 75) chain D residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 76) chain D residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 77) chain D residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 78) chain D residue 194 type sequence A description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 79) chain D residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 80) chain D residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 81) chain D residue 226 type sequence P description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 82) chain D residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 83) chain D residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 84) chain D residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 85) chain D residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 86) chain D residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 87) chain D residue 249 type sequence V description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 88) chain D residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 89) chain D residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 90) chain D residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 91) chain D residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 92) chain D residue 349 type sequence Q description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 93) chain D residue 352 type sequence K description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 94) chain D residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 95) chain D residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 96) chain A residue 269 type ACT_SITE sequence L description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 source Swiss-Prot : SWS_FT_FI1 97) chain B residue 268 type ACT_SITE sequence E description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 source Swiss-Prot : SWS_FT_FI1 98) chain C residue 268 type ACT_SITE sequence E description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 source Swiss-Prot : SWS_FT_FI1 99) chain D residue 269 type ACT_SITE sequence L description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 source Swiss-Prot : SWS_FT_FI1 100) chain A residue 337 type MOD_RES sequence P description Phosphothreonine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI8 101) chain B residue 336 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI8 102) chain C residue 336 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI8 103) chain D residue 337 type MOD_RES sequence P description Phosphothreonine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI8 104) chain A residue 295-306 type prosite sequence FYHQGQCCIAAS description ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FyHQGQCCIAAS source prosite : PS00070 105) chain A residue 267-274 type prosite sequence LELGGKSP description ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP source prosite : PS00687 106) chain A residue 413 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI9 107) chain B residue 412 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI9 108) chain C residue 412 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI9 109) chain D residue 413 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI9 110) chain A residue 170 type SITE sequence F description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI5 111) chain B residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI5 112) chain C residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI5 113) chain D residue 170 type SITE sequence F description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI5 114) chain A residue 91 type MOD_RES sequence L description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 115) chain B residue 127 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 116) chain B residue 251 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 117) chain B residue 352 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 118) chain B residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 119) chain B residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 120) chain B residue 418 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 121) chain B residue 494 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 122) chain C residue 90 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 123) chain C residue 127 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 124) chain C residue 251 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 125) chain A residue 128 type MOD_RES sequence T description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 126) chain C residue 352 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 127) chain C residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 128) chain C residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 129) chain C residue 418 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 130) chain C residue 494 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 131) chain D residue 91 type MOD_RES sequence L description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 132) chain D residue 128 type MOD_RES sequence T description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 133) chain D residue 252 type MOD_RES sequence L description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 134) chain D residue 353 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 135) chain D residue 367 type MOD_RES sequence L description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 136) chain A residue 252 type MOD_RES sequence L description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 137) chain D residue 410 type MOD_RES sequence F description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 138) chain D residue 419 type MOD_RES sequence R description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 139) chain D residue 495 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 140) chain A residue 353 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 141) chain A residue 367 type MOD_RES sequence L description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 142) chain A residue 410 type MOD_RES sequence F description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 143) chain A residue 419 type MOD_RES sequence R description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 144) chain A residue 495 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 145) chain B residue 90 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 146) chain A residue 303 type ACT_SITE sequence I description Nucleophile => ECO:0000303|PubMed:9862807 source Swiss-Prot : SWS_FT_FI2 147) chain B residue 302 type ACT_SITE sequence C description Nucleophile => ECO:0000303|PubMed:9862807 source Swiss-Prot : SWS_FT_FI2 148) chain C residue 302 type ACT_SITE sequence C description Nucleophile => ECO:0000303|PubMed:9862807 source Swiss-Prot : SWS_FT_FI2 149) chain D residue 303 type ACT_SITE sequence I description Nucleophile => ECO:0000303|PubMed:9862807 source Swiss-Prot : SWS_FT_FI2 150) chain A residue 167 type BINDING sequence P description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 151) chain B residue 245 type BINDING sequence G description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 152) chain B residue 348 type BINDING sequence E description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 153) chain B residue 399 type BINDING sequence E description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 154) chain C residue 166 type BINDING sequence I description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 155) chain C residue 192 type BINDING sequence K description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 156) chain C residue 225 type BINDING sequence G description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 157) chain C residue 245 type BINDING sequence G description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 158) chain C residue 348 type BINDING sequence E description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 159) chain C residue 399 type BINDING sequence E description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 160) chain D residue 167 type BINDING sequence P description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 161) chain A residue 193 type BINDING sequence P description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 162) chain D residue 193 type BINDING sequence P description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 163) chain D residue 226 type BINDING sequence P description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 164) chain D residue 246 type BINDING sequence S description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 165) chain D residue 349 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 166) chain D residue 400 type BINDING sequence I description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 167) chain A residue 226 type BINDING sequence P description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 168) chain A residue 246 type BINDING sequence S description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 169) chain A residue 349 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 170) chain A residue 400 type BINDING sequence I description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 171) chain B residue 166 type BINDING sequence I description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 172) chain B residue 192 type BINDING sequence K description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 173) chain B residue 225 type BINDING sequence G description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 174) chain A residue 269 type BINDING sequence L description BINDING => ECO:0000269|PubMed:26373694, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI4 175) chain B residue 268 type BINDING sequence E description BINDING => ECO:0000269|PubMed:26373694, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI4 176) chain C residue 268 type BINDING sequence E description BINDING => ECO:0000269|PubMed:26373694, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI4 177) chain D residue 269 type BINDING sequence L description BINDING => ECO:0000269|PubMed:26373694, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI4

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