eF-site ID 1cw3-C PDB Code 1cw3 Chain C click to enlarge Title HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH NAD+ AND MN2+ Classification OXIDOREDUCTASE Compound MITOCHONDRIAL ALDEHYDE DEHYDROGENASE Source null (ALDH2_HUMAN) Sequence C:  AVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGE VICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGR LLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVL KCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQII PWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVAN LIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGS TEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWA VEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARA KSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAK LLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQ ILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQAL QAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYT EVKTVTVKVPQKNS Description Functional site 1) chain C residue 39 type sequence T description BINDING SITE FOR RESIDUE MG C 3501 source : BC2 2) chain C residue 40 type sequence V description BINDING SITE FOR RESIDUE MG C 3501 source : BC2 3) chain C residue 109 type sequence D description BINDING SITE FOR RESIDUE MG C 3501 source : BC2 4) chain C residue 196 type sequence Q description BINDING SITE FOR RESIDUE MG C 3501 source : BC2 5) chain C residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 6) chain C residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 7) chain C residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 8) chain C residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 9) chain C residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 10) chain C residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 11) chain C residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 12) chain C residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 13) chain C residue 226 type sequence P description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 14) chain C residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 15) chain C residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 16) chain C residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 17) chain C residue 244 type sequence T description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 18) chain C residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 19) chain C residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 20) chain C residue 249 type sequence I description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 21) chain C residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 22) chain C residue 268 type sequence E description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 23) chain C residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 24) chain C residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 25) chain C residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 26) chain C residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 27) chain C residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 28) chain C residue 465 type sequence F description BINDING SITE FOR RESIDUE NAD C 3502 source : CC1 29) chain C residue 192 type catalytic sequence K description 803 source MCSA : MCSA3 30) chain C residue 268 type catalytic sequence E description 803 source MCSA : MCSA3 31) chain C residue 302 type catalytic sequence C description 803 source MCSA : MCSA3 32) chain C residue 399 type catalytic sequence E description 803 source MCSA : MCSA3 33) chain C residue 268 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI1 34) chain C residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI4 35) chain C residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 36) chain C residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 37) chain C residue 61 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 38) chain C residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 39) chain C residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 40) chain C residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 41) chain C residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 42) chain C residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 43) chain C residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 44) chain C residue 302 type ACT_SITE sequence C description Nucleophile source Swiss-Prot : SWS_FT_FI2 45) chain C residue 245 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3

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