eF-site ID 1bxs-C PDB Code 1bxs Chain C click to enlarge Title SHEEP LIVER CLASS 1 ALDEHYDE DEHYDROGENASE WITH NAD BOUND Classification OXIDOREDUCTASE Compound ALDEHYDE DEHYDROGENASE Source ORGANISM_COMMON: sheep; ORGANISM_SCIENTIFIC: Ovis aries; Sequence C:  DVPAPLTNLQFKYTKIFINNEWHSSVSGKKFPVFNPATEE KLCEVEEGDKEDVDKAVKAARQAFQIGSPWRTMDASERGR LLNKLADLIERDRLLLATMEAMNGGKLFSNAYLMDLGGCI KTLRYCAGWADKIQGRTIPMDGNFFTYTRSEPVGVCGQII PWNFPLLMFLWKIGPALSCGNTVVVKPAEQTPLTALHMGS LIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGS TEVGKLIKEAAGKSNLKRVSLELGGKSPCIVFADADLDNA VEFAHQGVFYHQGQCCIAASRLFVEESIYDEFVRRSVERA KKYVLGNPLTPGVSQGPQIDKEQYEKILDLIESGKKEGAK LECGGGPWGNKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQ IMKFKSLDDVIKRANNTFYGLSAGIFTNDIDKAITVSSAL QSGTVWVNCYSVVSAQCPFGGFKMSGNGRELGEYGFHEYT EVKTVTIKISQKNS Description Functional site 1) chain C residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 2) chain C residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 3) chain C residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 4) chain C residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 5) chain C residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 6) chain C residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 7) chain C residue 194 type sequence A description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 8) chain C residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 9) chain C residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 10) chain C residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 11) chain C residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 12) chain C residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 13) chain C residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 14) chain C residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 15) chain C residue 249 type sequence V description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 16) chain C residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 17) chain C residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 18) chain C residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 19) chain C residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 20) chain C residue 349 type sequence Q description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 21) chain C residue 352 type sequence K description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 22) chain C residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 23) chain C residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD C 550 source : AC3 24) chain C residue 412 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI9 25) chain C residue 268 type ACT_SITE sequence E description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 source Swiss-Prot : SWS_FT_FI1 26) chain C residue 302 type ACT_SITE sequence C description Nucleophile => ECO:0000303|PubMed:9862807 source Swiss-Prot : SWS_FT_FI2 27) chain C residue 166 type BINDING sequence I description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 28) chain C residue 192 type BINDING sequence K description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 29) chain C residue 225 type BINDING sequence G description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 30) chain C residue 245 type BINDING sequence G description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 31) chain C residue 348 type BINDING sequence E description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 32) chain C residue 399 type BINDING sequence E description BINDING => ECO:0000269|PubMed:26373694, ECO:0000269|PubMed:9862807, ECO:0007744|PDB:1BXS, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI3 33) chain C residue 268 type BINDING sequence E description BINDING => ECO:0000269|PubMed:26373694, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI4 34) chain C residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI5 35) chain C residue 90 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 36) chain C residue 127 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 37) chain C residue 251 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 38) chain C residue 352 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 39) chain C residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 40) chain C residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 41) chain C residue 418 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 42) chain C residue 494 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 43) chain C residue 336 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI8

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