eF-site ID 1a4z-C PDB Code 1a4z Chain C 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 C:  VPTPNQQPEVLYNQIFINNEWHDAVSKKTFPTVNPSTGDV ICHVAEGDKADVDRAVKAARAAFQLGSPWRRMDASERGRL LNRLADLIERDRTYLAALETLDNGKPYIISYLVDLDMVLK CLRYYAGWADKYHGKTIPIDGDYFSYTRHEPVGVCGQIIP WNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANL IKEAGFPPGVVNVIPGFGPTAGAAIASHEDVDKVAFTGST EVGHLIQVAAGKSNLKRVTLEIGGKSPNIIMSDADMDWAV EQAHFALFFNQGQCCCAGSRTFVQEDIYAEFVERSVARAK SRVVGNPFDSRTEQGPQVDETQFKKVLGYIKSGKEEGLKL LCGGGAAADRGYFIQPTVFGDLQDGMTIAKEEIFGPVMQI LKFKSMEEVVGRANNSKYGLAAAVFTKDLDKANYLSQALQ AGTVWVNCYDVFGAQSPFGGYKLSGSGRELGEYGLQAYTE VKTVTVRVPQKNS Description Functional site 1) chain C residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 2) chain C residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 3) chain C residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 4) chain C residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 5) chain C residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 6) chain C residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 7) chain C residue 194 type sequence A description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 8) chain C residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 9) chain C residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 10) chain C residue 226 type sequence P description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 11) chain C residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 12) chain C residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 13) chain C residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 14) chain C residue 244 type sequence T description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 15) chain C residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 16) chain C residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 17) chain C residue 249 type sequence V description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 18) chain C residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 19) chain C residue 268 type sequence E description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 20) chain C residue 269 type sequence I description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 21) chain C residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 22) chain C residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 23) chain C residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 24) chain C residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 25) chain C residue 268 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:9195888 source Swiss-Prot : SWS_FT_FI1 26) chain C residue 302 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:9195888 source Swiss-Prot : SWS_FT_FI2 27) chain C residue 166 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 28) chain C residue 192 type BINDING sequence K description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 29) chain C residue 225 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 30) chain C residue 245 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 31) chain C residue 268 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 32) chain C residue 399 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 33) chain C residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000269|PubMed:9195888 source Swiss-Prot : SWS_FT_FI4 34) chain C residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 35) chain C residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 36) chain C residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 37) chain C residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 38) chain C residue 358 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 39) chain C residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 40) chain C residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 41) chain C residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 42) chain C residue 424 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 43) chain C residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5

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