eF-site ID 1a4z-A PDB Code 1a4z Chain A click to enlarge Title ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA COMPLEX WITH NAD (REDUCED) AND SAMARIUM (III) Classification OXIDOREDUCTASE Compound ALDEHYDE DEHYDROGENASE Source ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus; Sequence A:  VPTPNQQPEVLYNQIFINNEWHDAVSKKTFPTVNPSTGDV ICHVAEGDKADVDRAVKAARAAFQLGSPWRRMDASERGRL LNRLADLIERDRTYLAALETLDNGKPYIISYLVDLDMVLK CLRYYAGWADKYHGKTIPIDGDYFSYTRHEPVGVCGQIIP WNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANL IKEAGFPPGVVNVIPGFGPTAGAAIASHEDVDKVAFTGST EVGHLIQVAAGKSNLKRVTLEIGGKSPNIIMSDADMDWAV EQAHFALFFNQGQCCCAGSRTFVQEDIYAEFVERSVARAK SRVVGNPFDSRTEQGPQVDETQFKKVLGYIKSGKEEGLKL LCGGGAAADRGYFIQPTVFGDLQDGMTIAKEEIFGPVMQI LKFKSMEEVVGRANNSKYGLAAAVFTKDLDKANYLSQALQ AGTVWVNCYDVFGAQSPFGGYKLSGSGRELGEYGLQAYTE VKTVTVRVPQKNS Description Functional site 1) chain A residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 2) chain A residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 3) chain A residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 4) chain A residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 5) chain A residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 6) chain A residue 174 type sequence M description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 7) chain A residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 8) chain A residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 9) chain A residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 10) chain A residue 226 type sequence P description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 11) chain A residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 12) chain A residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 13) chain A residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 14) chain A residue 244 type sequence T description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 15) chain A residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 16) chain A residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 17) chain A residue 249 type sequence V description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 18) chain A residue 252 type sequence L description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 19) chain A residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 20) chain A residue 268 type sequence E description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 21) chain A residue 269 type sequence I description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 22) chain A residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 23) chain A residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 24) chain A residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 25) chain A residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 26) chain A residue 268 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:9195888 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 302 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:9195888 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 192 type BINDING sequence K description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 29) chain A residue 225 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 30) chain A residue 245 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 31) chain A residue 268 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 32) chain A residue 399 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 33) chain A residue 166 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 34) chain A residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000269|PubMed:9195888 source Swiss-Prot : SWS_FT_FI4 35) chain A residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 36) chain A residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 37) chain A residue 351 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 358 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 40) chain A residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 41) chain A residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 42) chain A residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 43) chain A residue 424 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 44) chain A residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 45) chain A residue 295-306 type prosite sequence FFNQGQCCCAGS description ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfNQGQCCCAGS source prosite : PS00070 46) chain A residue 267-274 type prosite sequence LEIGGKSP description ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LEIGGKSP source prosite : PS00687

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