eF-site ID 1cw3-G PDB Code 1cw3 Chain G click to enlarge Title HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH NAD+ AND MN2+ Classification OXIDOREDUCTASE Compound MITOCHONDRIAL ALDEHYDE DEHYDROGENASE Source null (ALDH2_HUMAN) Sequence G:  AVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGE VICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGR LLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVL KCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQII PWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVAN LIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGS TEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWA VEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARA KSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAK LLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQ ILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQAL QAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYT EVKTVTVKVPQKNS Description Functional site 1) chain G residue 39 type sequence T description BINDING SITE FOR RESIDUE MG G 7501 source : BC6 2) chain G residue 40 type sequence V description BINDING SITE FOR RESIDUE MG G 7501 source : BC6 3) chain G residue 109 type sequence D description BINDING SITE FOR RESIDUE MG G 7501 source : BC6 4) chain G residue 196 type sequence Q description BINDING SITE FOR RESIDUE MG G 7501 source : BC6 5) chain G residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 6) chain G residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 7) chain G residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 8) chain G residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 9) chain G residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 10) chain G residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 11) chain G residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 12) chain G residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 13) chain G residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 14) chain G residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 15) chain G residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 16) chain G residue 244 type sequence T description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 17) chain G residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 18) chain G residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 19) chain G residue 249 type sequence I description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 20) chain G residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 21) chain G residue 268 type sequence E description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 22) chain G residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 23) chain G residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 24) chain G residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 25) chain G residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 26) chain G residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 27) chain G residue 465 type sequence F description BINDING SITE FOR RESIDUE NAD G 7502 source : CC5 28) chain G residue 192 type catalytic sequence K description 803 source MCSA : MCSA7 29) chain G residue 268 type catalytic sequence E description 803 source MCSA : MCSA7 30) chain G residue 302 type catalytic sequence C description 803 source MCSA : MCSA7 31) chain G residue 399 type catalytic sequence E description 803 source MCSA : MCSA7 32) chain G residue 268 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI1 33) chain G residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI4 34) chain G residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 35) chain G residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 36) chain G residue 61 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 37) chain G residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 38) chain G residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 39) chain G residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 40) chain G residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 41) chain G residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 42) chain G residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 43) chain G residue 302 type ACT_SITE sequence C description Nucleophile source Swiss-Prot : SWS_FT_FI2 44) chain G residue 245 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3

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