eF-site ID 1ag8-C PDB Code 1ag8 Chain C click to enlarge Title ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA 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 (1)  ALDEHYDE DEHYDROGENASE Functional site 1) chain C residue 268 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:9195888 source Swiss-Prot : SWS_FT_FI1 2) chain C residue 302 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:9195888 source Swiss-Prot : SWS_FT_FI2 3) chain C residue 166 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 4) chain C residue 192 type BINDING sequence K description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 5) chain C residue 225 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 6) chain C residue 245 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 7) chain C residue 268 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 8) chain C residue 399 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 9) chain C residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000269|PubMed:9195888 source Swiss-Prot : SWS_FT_FI4 10) chain C residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 11) chain C residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 12) chain C residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 13) chain C residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 14) chain C residue 358 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 15) chain C residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 16) chain C residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 17) chain C residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 18) chain C residue 424 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 19) chain C residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5

Display surface Download Links