eF-site ID 1cw3-E PDB Code 1cw3 Chain E click to enlarge Title HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH NAD+ AND MN2+ Classification OXIDOREDUCTASE Compound MITOCHONDRIAL ALDEHYDE DEHYDROGENASE Source null (ALDH2_HUMAN) Sequence E:  AVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGE VICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGR LLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVL KCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQII PWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVAN LIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGS TEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWA VEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARA KSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAK LLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQ ILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQAL QAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYT EVKTVTVKVPQKNS Description Functional site 1) chain E residue 39 type sequence T description BINDING SITE FOR RESIDUE MG E 5501 source : BC4 2) chain E residue 40 type sequence V description BINDING SITE FOR RESIDUE MG E 5501 source : BC4 3) chain E residue 109 type sequence D description BINDING SITE FOR RESIDUE MG E 5501 source : BC4 4) chain E residue 196 type sequence Q description BINDING SITE FOR RESIDUE MG E 5501 source : BC4 5) chain E residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 6) chain E residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 7) chain E residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 8) chain E residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 9) chain E residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 10) chain E residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 11) chain E residue 194 type sequence A description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 12) chain E residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 13) chain E residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 14) chain E residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 15) chain E residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 16) chain E residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 17) chain E residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 18) chain E residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 19) chain E residue 249 type sequence I description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 20) chain E residue 268 type sequence E description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 21) chain E residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 22) chain E residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 23) chain E residue 349 type sequence Q description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 24) chain E residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 25) chain E residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD E 5502 source : CC3 26) chain E residue 192 type catalytic sequence K description 803 source MCSA : MCSA5 27) chain E residue 268 type catalytic sequence E description 803 source MCSA : MCSA5 28) chain E residue 302 type catalytic sequence C description 803 source MCSA : MCSA5 29) chain E residue 399 type catalytic sequence E description 803 source MCSA : MCSA5 30) chain E residue 268 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI1 31) chain E residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI4 32) chain E residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 33) chain E residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 34) chain E residue 61 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 35) chain E residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 36) chain E residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 37) chain E residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 38) chain E residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 39) chain E residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 40) chain E residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 41) chain E residue 302 type ACT_SITE sequence C description Nucleophile source Swiss-Prot : SWS_FT_FI2 42) chain E residue 245 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3

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