eF-site ID 1cw3-H PDB Code 1cw3 Chain H click to enlarge Title HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH NAD+ AND MN2+ Classification OXIDOREDUCTASE Compound MITOCHONDRIAL ALDEHYDE DEHYDROGENASE Source Homo sapiens (Human) (ALDH2_HUMAN) Sequence H:  AVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGE VICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGR LLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVL KCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQII PWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVAN LIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGS TEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWA VEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARA KSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAK LLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQ ILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQAL QAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYT EVKTVTVKVPQKNS Description Functional site 1) chain H residue 39 type sequence T description BINDING SITE FOR RESIDUE MG H 8501 source : BC7 2) chain H residue 40 type sequence V description BINDING SITE FOR RESIDUE MG H 8501 source : BC7 3) chain H residue 109 type sequence D description BINDING SITE FOR RESIDUE MG H 8501 source : BC7 4) chain H residue 196 type sequence Q description BINDING SITE FOR RESIDUE MG H 8501 source : BC7 5) chain H residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 6) chain H residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 7) chain H residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 8) chain H residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 9) chain H residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 10) chain H residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 11) chain H residue 194 type sequence A description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 12) chain H residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 13) chain H residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 14) chain H residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 15) chain H residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 16) chain H residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 17) chain H residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 18) chain H residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 19) chain H residue 249 type sequence I description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 20) chain H residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 21) chain H residue 268 type sequence E description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 22) chain H residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 23) chain H residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 24) chain H residue 349 type sequence Q description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 25) chain H residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 26) chain H residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD H 8502 source : CC6 27) chain H residue 268 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI1 28) chain H residue 302 type ACT_SITE sequence C description Nucleophile source Swiss-Prot : SWS_FT_FI2 29) chain H residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI4 30) chain H residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 31) chain H residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 32) chain H residue 61 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 33) chain H residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 34) chain H residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 35) chain H residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 36) chain H residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 37) chain H residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 38) chain H residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 39) chain H residue 192 type catalytic sequence K description 803 source MCSA : MCSA8 40) chain H residue 268 type catalytic sequence E description 803 source MCSA : MCSA8 41) chain H residue 302 type catalytic sequence C description 803 source MCSA : MCSA8 42) chain H residue 399 type catalytic sequence E description 803 source MCSA : MCSA8 43) chain H residue 245 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3

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