eF-site ID 1cw3-A PDB Code 1cw3 Chain A 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 A:  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 A residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 6) chain A residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 7) chain A residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 8) chain A residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 9) chain A residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 10) chain A residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 11) chain A residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 12) chain A residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 13) chain A residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 14) chain A residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 15) chain A residue 244 type sequence T description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 16) chain A residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 17) chain A residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 18) chain A residue 249 type sequence I description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 19) chain A residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 20) chain A residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 21) chain A residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 22) chain A residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 23) chain A residue 349 type sequence Q description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 24) chain A residue 352 type sequence K description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 25) chain A residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 26) chain A residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD A 1502 source : BC8 27) chain A residue 268 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI1 28) chain A residue 302 type ACT_SITE sequence C description Nucleophile source Swiss-Prot : SWS_FT_FI2 29) chain A residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI4 30) chain A residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 31) chain A residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 32) chain A residue 61 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 33) chain A residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 34) chain A residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 35) chain A residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 36) chain A residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 37) chain A residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 38) chain A residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 39) chain A residue 192 type catalytic sequence K description 803 source MCSA : MCSA1 40) chain A residue 268 type catalytic sequence E description 803 source MCSA : MCSA1 41) chain A residue 302 type catalytic sequence C description 803 source MCSA : MCSA1 42) chain A residue 399 type catalytic sequence E description 803 source MCSA : MCSA1 43) chain A residue 295-306 type prosite sequence FFNQGQCCCAGS description ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfNQGQCCCAGS source prosite : PS00070 44) chain A residue 267-274 type prosite sequence LELGGKSP description ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP source prosite : PS00687 45) chain A residue 245 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3

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