eF-site ID 1a4z-B PDB Code 1a4z Chain B 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 B:  VPTPNQQPEVLYNQIFINNEWHDAVSKKTFPTVNPSTGDV ICHVAEGDKADVDRAVKAARAAFQLGSPWRRMDASERGRL LNRLADLIERDRTYLAALETLDNGKPYIISYLVDLDMVLK CLRYYAGWADKYHGKTIPIDGDYFSYTRHEPVGVCGQIIP WNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANL IKEAGFPPGVVNVIPGFGPTAGAAIASHEDVDKVAFTGST EVGHLIQVAAGKSNLKRVTLEIGGKSPNIIMSDADMDWAV EQAHFALFFNQGQCCCAGSRTFVQEDIYAEFVERSVARAK SRVVGNPFDSRTEQGPQVDETQFKKVLGYIKSGKEEGLKL LCGGGAAADRGYFIQPTVFGDLQDGMTIAKEEIFGPVMQI LKFKSMEEVVGRANNSKYGLAAAVFTKDLDKANYLSQALQ AGTVWVNCYDVFGAQSPFGGYKLSGSGRELGEYGLQAYTE VKTVTVRVPQKNS Description Functional site 1) chain B residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 2) chain B residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 3) chain B residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 4) chain B residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 5) chain B residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 6) chain B residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 7) chain B residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 8) chain B residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 9) chain B residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 10) chain B residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 11) chain B residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 12) chain B residue 244 type sequence T description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 13) chain B residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 14) chain B residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 15) chain B residue 249 type sequence V description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 16) chain B residue 252 type sequence L description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 17) chain B residue 268 type sequence E description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 18) chain B residue 269 type sequence I description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 19) chain B residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 20) chain B residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 21) chain B residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 22) chain B residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 23) chain B residue 268 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:9195888 source Swiss-Prot : SWS_FT_FI1 24) chain B residue 302 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:9195888 source Swiss-Prot : SWS_FT_FI2 25) chain B residue 245 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 26) chain B residue 268 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 27) chain B residue 399 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 28) chain B residue 166 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 29) chain B residue 192 type BINDING sequence K description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 30) chain B residue 225 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 31) chain B residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000269|PubMed:9195888 source Swiss-Prot : SWS_FT_FI4 32) chain B residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 33) chain B residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 34) chain B residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 35) chain B residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 36) chain B residue 358 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 37) chain B residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 38) chain B residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 39) chain B residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 40) chain B residue 424 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 41) chain B residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5

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