eF-site ID 1cw3-ABCDEFGH PDB Code 1cw3 Chain A, B, C, D, E, F, G, H click to enlarge Title HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH NAD+ AND MN2+ Classification OXIDOREDUCTASE Compound MITOCHONDRIAL ALDEHYDE DEHYDROGENASE Source null (ALDH2_HUMAN) Sequence A:  AVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGE VICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGR LLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVL KCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQII PWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVAN LIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGS TEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWA VEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARA KSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAK LLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQ ILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQAL QAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYT EVKTVTVKVPQKNS B:  AVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGE VICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGR LLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVL KCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQII PWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVAN LIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGS TEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWA VEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARA KSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAK LLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQ ILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQAL QAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYT EVKTVTVKVPQKNS C:  AVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGE VICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGR LLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVL KCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQII PWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVAN LIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGS TEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWA VEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARA KSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAK LLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQ ILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQAL QAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYT EVKTVTVKVPQKNS D:  AVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGE VICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGR LLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVL KCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQII PWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVAN LIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGS TEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWA VEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARA KSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAK LLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQ ILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQAL QAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYT EVKTVTVKVPQKNS E:  AVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGE VICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGR LLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVL KCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQII PWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVAN LIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGS TEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWA VEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARA KSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAK LLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQ ILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQAL QAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYT EVKTVTVKVPQKNS F:  AVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGE VICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGR LLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVL KCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQII PWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVAN LIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGS TEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWA VEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARA KSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAK LLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQ ILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQAL QAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYT EVKTVTVKVPQKNS G:  AVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGE VICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGR LLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVL KCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQII PWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVAN LIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGS TEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWA VEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARA KSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAK LLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQ ILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQAL QAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYT EVKTVTVKVPQKNS H:  AVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGE VICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGR LLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVL KCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQII PWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVAN LIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGS TEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWA VEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARA KSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAK LLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQ ILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQAL QAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYT EVKTVTVKVPQKNS Description Functional site 1) chain A residue 39 type sequence T description BINDING SITE FOR RESIDUE MG A 1501 source : AC9 2) chain A residue 40 type sequence V description BINDING SITE FOR RESIDUE MG A 1501 source : AC9 3) chain A residue 109 type sequence D description BINDING SITE FOR RESIDUE MG A 1501 source : AC9 4) chain A residue 196 type sequence Q description BINDING SITE FOR RESIDUE MG A 1501 source : AC9 5) chain B residue 39 type sequence T description BINDING SITE FOR RESIDUE MG B 2501 source : BC1 6) chain B residue 40 type sequence V description BINDING SITE FOR RESIDUE MG B 2501 source : BC1 7) chain B residue 109 type sequence D description BINDING SITE FOR RESIDUE MG B 2501 source : BC1 8) chain B residue 196 type sequence Q description BINDING SITE FOR RESIDUE MG B 2501 source : BC1 9) chain C residue 39 type sequence T description BINDING SITE FOR RESIDUE MG C 3501 source : BC2 10) chain C residue 40 type sequence V description BINDING SITE FOR RESIDUE MG C 3501 source : BC2 11) chain C residue 109 type sequence D description BINDING SITE FOR RESIDUE MG C 3501 source : BC2 12) chain C residue 196 type sequence Q description BINDING SITE FOR RESIDUE MG C 3501 source : BC2 13) chain D residue 40 type sequence V description BINDING SITE FOR RESIDUE MG D 4501 source : BC3 14) chain D residue 109 type sequence D description BINDING SITE FOR RESIDUE MG D 4501 source : BC3 15) chain D residue 196 type sequence Q description BINDING SITE FOR RESIDUE MG D 4501 source : BC3 16) chain E residue 39 type sequence T description BINDING SITE FOR RESIDUE MG E 5501 source : BC4 17) chain E residue 40 type sequence V description BINDING SITE FOR RESIDUE MG E 5501 source : BC4 18) chain E residue 109 type sequence D description BINDING SITE FOR RESIDUE MG E 5501 source : BC4 19) chain E residue 196 type sequence Q description BINDING SITE FOR RESIDUE MG E 5501 source : BC4 20) chain F residue 39 type sequence T description BINDING SITE FOR RESIDUE MG F 6501 source : BC5 21) chain F residue 40 type sequence V description BINDING SITE FOR RESIDUE MG F 6501 source : BC5 22) chain F residue 109 type sequence D description BINDING SITE FOR RESIDUE MG F 6501 source : BC5 23) chain F residue 196 type sequence Q description BINDING SITE FOR RESIDUE MG F 6501 source : BC5 24) chain G residue 39 type sequence T description BINDING SITE FOR RESIDUE MG G 7501 source : BC6 25) chain G residue 40 type sequence V description BINDING SITE FOR RESIDUE MG G 7501 source : BC6 26) chain G residue 109 type sequence D description BINDING SITE FOR RESIDUE MG G 7501 source : BC6 27) chain G residue 196 type sequence Q description BINDING SITE FOR RESIDUE MG G 7501 source : BC6 28) chain H residue 39 type sequence T description BINDING SITE FOR RESIDUE MG H 8501 source : BC7 29) chain H residue 40 type sequence V description BINDING SITE FOR RESIDUE MG H 8501 source : BC7 30) chain H residue 109 type sequence D description BINDING SITE FOR RESIDUE MG H 8501 source : BC7 31) chain H residue 196 type sequence Q description BINDING SITE FOR RESIDUE MG H 8501 source : BC7 32) chain A residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 33) chain A residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 34) chain A residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 35) chain A residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 36) chain A residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 37) chain A residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 38) chain A residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 39) chain A residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 40) chain A residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 41) chain A residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 42) chain A residue 244 type sequence T description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 43) chain A residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 44) chain A residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 45) chain A residue 249 type sequence I description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 46) chain A residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 47) chain A residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 48) chain A residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 49) chain A residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 50) chain A residue 349 type sequence Q description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 51) chain A residue 352 type sequence K description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 52) chain A residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 53) chain A residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 54) chain B residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 55) chain B residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 56) chain B residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 57) chain B residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 58) chain B residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 59) chain B residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 60) chain B residue 194 type sequence A description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 61) chain B residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 62) chain B residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 63) chain B residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 64) chain B residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 65) chain B residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 66) chain B residue 244 type sequence T description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 67) chain B residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 68) chain B residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 69) chain B residue 249 type sequence I description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 70) chain B residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 71) chain B residue 268 type sequence E description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 72) chain B residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 73) chain B residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 74) chain B residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 75) chain B residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 76) chain B residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 77) chain B residue 427 type sequence L description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 78) chain B residue 465 type sequence F description BINDING SITE FOR RESIDUE NAD B 2502 source : BC9 79) chain C residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 80) chain C residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 81) chain C residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 82) chain C residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 83) chain C residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 84) chain C residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 85) chain C residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 86) chain C residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 87) chain C residue 226 type sequence P description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 88) chain C residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 89) chain C residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 90) chain C residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 91) chain C residue 244 type sequence T description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 92) chain C residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 93) chain C residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 94) chain C residue 249 type sequence I description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 95) chain C residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 96) chain C residue 268 type sequence E description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 97) chain C residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 98) chain C residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 99) chain C residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 100) chain C residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 101) chain C residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 102) chain C residue 465 type sequence F description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 103) chain D residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 104) chain D residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 105) chain D residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 106) chain D residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 107) chain D residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 108) chain D residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 109) chain D residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 110) chain D residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 111) chain D residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 112) chain D residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 113) chain D residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 114) chain D residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 115) chain D residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 116) chain D residue 249 type sequence I description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 117) chain D residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 118) chain D residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 119) chain D residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 120) chain D residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 121) chain D residue 349 type sequence Q description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 122) chain D residue 352 type sequence K description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 123) chain D residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 124) chain D residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 125) chain E residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 126) chain E residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 127) chain E residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 128) chain E residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 129) chain E residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 130) chain E residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 131) chain E residue 194 type sequence A description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 132) chain E residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 133) chain E residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 134) chain E residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 135) chain E residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 136) chain E residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 137) chain E residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 138) chain E residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 139) chain E residue 249 type sequence I description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 140) chain E residue 268 type sequence E description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 141) chain E residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 142) chain E residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 143) chain E residue 349 type sequence Q description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 144) chain E residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 145) chain E residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 146) chain F residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 147) chain F residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 148) chain F residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 149) chain F residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 150) chain F residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 151) chain F residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 152) chain F residue 194 type sequence A description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 153) chain F residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 154) chain F residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 155) chain F residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 156) chain F residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 157) chain F residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 158) chain F residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 159) chain F residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 160) chain F residue 249 type sequence I description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 161) chain F residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 162) chain F residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 163) chain F residue 349 type sequence Q description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 164) chain F residue 352 type sequence K description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 165) chain F residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 166) chain G residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 167) chain G residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 168) chain G residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 169) chain G residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 170) chain G residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 171) chain G residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 172) chain G residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 173) chain G residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 174) chain G residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 175) chain G residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 176) chain G residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 177) chain G residue 244 type sequence T description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 178) chain G residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 179) chain G residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 180) chain G residue 249 type sequence I description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 181) chain G residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 182) chain G residue 268 type sequence E description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 183) chain G residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 184) chain G residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 185) chain G residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 186) chain G residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 187) chain G residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 188) chain G residue 465 type sequence F description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 189) chain H residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 190) chain H residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 191) chain H residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 192) chain H residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 193) chain H residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 194) chain H residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 195) chain H residue 194 type sequence A description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 196) chain H residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 197) chain H residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 198) chain H residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 199) chain H residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 200) chain H residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 201) chain H residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 202) chain H residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 203) chain H residue 249 type sequence I description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 204) chain H residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 205) chain H residue 268 type sequence E description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 206) chain H residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 207) chain H residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 208) chain H residue 349 type sequence Q description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 209) chain H residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 210) chain H residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 211) chain A residue 192 type catalytic sequence K description 803 source MCSA : MCSA1 212) chain A residue 268 type catalytic sequence E description 803 source MCSA : MCSA1 213) chain A residue 302 type catalytic sequence C description 803 source MCSA : MCSA1 214) chain A residue 399 type catalytic sequence E description 803 source MCSA : MCSA1 215) chain B residue 192 type catalytic sequence K description 803 source MCSA : MCSA2 216) chain B residue 268 type catalytic sequence E description 803 source MCSA : MCSA2 217) chain B residue 302 type catalytic sequence C description 803 source MCSA : MCSA2 218) chain B residue 399 type catalytic sequence E description 803 source MCSA : MCSA2 219) chain C residue 192 type catalytic sequence K description 803 source MCSA : MCSA3 220) chain C residue 268 type catalytic sequence E description 803 source MCSA : MCSA3 221) chain C residue 302 type catalytic sequence C description 803 source MCSA : MCSA3 222) chain C residue 399 type catalytic sequence E description 803 source MCSA : MCSA3 223) chain D residue 192 type catalytic sequence K description 803 source MCSA : MCSA4 224) chain D residue 268 type catalytic sequence E description 803 source MCSA : MCSA4 225) chain D residue 302 type catalytic sequence C description 803 source MCSA : MCSA4 226) chain D residue 399 type catalytic sequence E description 803 source MCSA : MCSA4 227) chain E residue 192 type catalytic sequence K description 803 source MCSA : MCSA5 228) chain E residue 268 type catalytic sequence E description 803 source MCSA : MCSA5 229) chain E residue 302 type catalytic sequence C description 803 source MCSA : MCSA5 230) chain E residue 399 type catalytic sequence E description 803 source MCSA : MCSA5 231) chain F residue 192 type catalytic sequence K description 803 source MCSA : MCSA6 232) chain F residue 268 type catalytic sequence E description 803 source MCSA : MCSA6 233) chain F residue 302 type catalytic sequence C description 803 source MCSA : MCSA6 234) chain F residue 399 type catalytic sequence E description 803 source MCSA : MCSA6 235) chain G residue 192 type catalytic sequence K description 803 source MCSA : MCSA7 236) chain G residue 268 type catalytic sequence E description 803 source MCSA : MCSA7 237) chain G residue 302 type catalytic sequence C description 803 source MCSA : MCSA7 238) chain G residue 399 type catalytic sequence E description 803 source MCSA : MCSA7 239) chain H residue 192 type catalytic sequence K description 803 source MCSA : MCSA8 240) chain H residue 268 type catalytic sequence E description 803 source MCSA : MCSA8 241) chain H residue 302 type catalytic sequence C description 803 source MCSA : MCSA8 242) chain H residue 399 type catalytic sequence E description 803 source MCSA : MCSA8 243) chain A residue 268 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI1 244) chain D residue 268 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI1 245) chain E residue 268 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI1 246) chain F residue 268 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI1 247) chain G residue 268 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI1 248) chain H residue 268 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI1 249) chain B residue 268 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI1 250) chain C residue 268 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI1 251) chain B residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI4 252) chain C residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI4 253) chain D residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI4 254) chain E residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI4 255) chain F residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI4 256) chain G residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI4 257) chain H residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI4 258) chain A residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI4 259) chain A residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 260) chain A residue 61 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 261) chain A residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 262) chain A residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 263) chain A residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 264) chain A residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 265) chain A residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 266) chain A residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 267) chain B residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 268) chain B residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 269) chain B residue 61 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 270) chain B residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 271) chain B residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 272) chain B residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 273) chain B residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 274) chain B residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 275) chain B residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 276) chain C residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 277) chain C residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 278) chain C residue 61 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 279) chain C residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 280) chain C residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 281) chain C residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 282) chain C residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 283) chain C residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 284) chain C residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 285) chain D residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 286) chain D residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 287) chain D residue 61 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 288) chain D residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 289) chain D residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 290) chain D residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 291) chain D residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 292) chain D residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 293) chain D residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 294) chain E residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 295) chain E residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 296) chain E residue 61 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 297) chain E residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 298) chain E residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 299) chain E residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 300) chain E residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 301) chain E residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 302) chain E residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 303) chain F residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 304) chain F residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 305) chain F residue 61 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 306) chain F residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 307) chain F residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 308) chain F residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 309) chain F residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 310) chain F residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 311) chain F residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 312) chain G residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 313) chain G residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 314) chain G residue 61 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 315) chain G residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 316) chain G residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 317) chain G residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 318) chain G residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 319) chain G residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 320) chain G residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 321) chain H residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 322) chain H residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 323) chain H residue 61 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 324) chain H residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 325) chain H residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 326) chain H residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 327) chain H residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 328) chain H residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 329) chain H residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 330) chain A residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 331) chain A residue 295-306 type prosite sequence FFNQGQCCCAGS description ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfNQGQCCCAGS source prosite : PS00070 332) chain A residue 267-274 type prosite sequence LELGGKSP description ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP source prosite : PS00687 333) chain B residue 302 type ACT_SITE sequence C description Nucleophile source Swiss-Prot : SWS_FT_FI2 334) chain C residue 302 type ACT_SITE sequence C description Nucleophile source Swiss-Prot : SWS_FT_FI2 335) chain D residue 302 type ACT_SITE sequence C description Nucleophile source Swiss-Prot : SWS_FT_FI2 336) chain E residue 302 type ACT_SITE sequence C description Nucleophile source Swiss-Prot : SWS_FT_FI2 337) chain F residue 302 type ACT_SITE sequence C description Nucleophile source Swiss-Prot : SWS_FT_FI2 338) chain G residue 302 type ACT_SITE sequence C description Nucleophile source Swiss-Prot : SWS_FT_FI2 339) chain H residue 302 type ACT_SITE sequence C description Nucleophile source Swiss-Prot : SWS_FT_FI2 340) chain A residue 302 type ACT_SITE sequence C description Nucleophile source Swiss-Prot : SWS_FT_FI2 341) chain B residue 245 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 342) chain C residue 245 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 343) chain D residue 245 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 344) chain E residue 245 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 345) chain F residue 245 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 346) chain G residue 245 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 347) chain H residue 245 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 348) chain A residue 245 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3

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