eF-site ID 1cw3-F PDB Code 1cw3 Chain F 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 F:  AVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGE VICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGR LLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVL KCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQII PWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVAN LIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGS TEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWA VEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARA KSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAK LLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQ ILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQAL QAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYT EVKTVTVKVPQKNS Description Functional site 1) chain F residue 39 type sequence T description BINDING SITE FOR RESIDUE MG F 6501 source : BC5 2) chain F residue 40 type sequence V description BINDING SITE FOR RESIDUE MG F 6501 source : BC5 3) chain F residue 109 type sequence D description BINDING SITE FOR RESIDUE MG F 6501 source : BC5 4) chain F residue 196 type sequence Q description BINDING SITE FOR RESIDUE MG F 6501 source : BC5 5) chain F residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 6) chain F residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 7) chain F residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 8) chain F residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 9) chain F residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 10) chain F residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 11) chain F residue 194 type sequence A description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 12) chain F residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 13) chain F residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 14) chain F residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 15) chain F residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 16) chain F residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 17) chain F residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 18) chain F residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 19) chain F residue 249 type sequence I description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 20) chain F residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 21) chain F residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 22) chain F residue 349 type sequence Q description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 23) chain F residue 352 type sequence K description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 24) chain F residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD F 6502 source : CC4 25) chain F residue 192 type catalytic sequence K description 803 source MCSA : MCSA6 26) chain F residue 268 type catalytic sequence E description 803 source MCSA : MCSA6 27) chain F residue 302 type catalytic sequence C description 803 source MCSA : MCSA6 28) chain F residue 399 type catalytic sequence E description 803 source MCSA : MCSA6 29) chain F residue 268 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI1 30) chain F residue 302 type ACT_SITE sequence C description Nucleophile source Swiss-Prot : SWS_FT_FI2 31) chain F residue 245 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 32) chain F residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI4 33) chain F residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 34) chain F residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 35) chain F residue 61 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 36) chain F residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 37) chain F residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 38) chain F residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 39) chain F residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 40) chain F residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 41) chain F residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5

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