eF-site ID 1bxs-D PDB Code 1bxs Chain D 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 D:  DVPAPLTNLQFKYTKIFINNEWHSSVSGKKFPVFNPATEE KLCEVEEGDKEDVDKAVKAARQAFQIGSPWRTMDASERGR LLNKLADLIERDRLLLATMEAMNGGKLFSNAYLMDLGGCI KTLRYCAGWADKIQGRTIPMDGNFFTYTRSEPVGVCGQII PWNFPLLMFLWKIGPALSCGNTVVVKPAEQTPLTALHMGS LIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGS TEVGKLIKEAAGKSNLKRVSLELGGKSPCIVFADADLDNA VEFAHQGVFYHQGQCCIAASRLFVEESIYDEFVRRSVERA KKYVLGNPLTPGVSQGPQIDKEQYEKILDLIESGKKEGAK LECGGGPWGNKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQ IMKFKSLDDVIKRANNTFYGLSAGIFTNDIDKAITVSSAL QSGTVWVNCYSVVSAQCPFGGFKMSGNGRELGEYGFHEYT EVKTVTIKISQKNS Description Functional site 1) chain D residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 2) chain D residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 3) chain D residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 4) chain D residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 5) chain D residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 6) chain D residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 7) chain D residue 194 type sequence A description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 8) chain D residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 9) chain D residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 10) chain D residue 226 type sequence P description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 11) chain D residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 12) chain D residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 13) chain D residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 14) chain D residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 15) chain D residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 16) chain D residue 249 type sequence V description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 17) chain D residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 18) chain D residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 19) chain D residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 20) chain D residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 21) chain D residue 349 type sequence Q description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 22) chain D residue 352 type sequence K description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 23) chain D residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 24) chain D residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD D 550 source : AC4 25) chain D residue 269 type ACT_SITE sequence L description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 source Swiss-Prot : SWS_FT_FI1 26) chain D residue 303 type ACT_SITE sequence I description Nucleophile => ECO:0000303|PubMed:9862807 source Swiss-Prot : SWS_FT_FI2 27) chain D residue 167 type BINDING sequence P 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 D residue 193 type BINDING sequence P 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 D residue 226 type BINDING sequence P 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 D residue 246 type BINDING sequence S 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 D residue 349 type BINDING sequence Q 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 D residue 400 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 33) chain D residue 269 type BINDING sequence L description BINDING => ECO:0000269|PubMed:26373694, ECO:0007744|PDB:5AC0 source Swiss-Prot : SWS_FT_FI4 34) chain D residue 170 type SITE sequence F description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI5 35) chain D residue 91 type MOD_RES sequence L description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 36) chain D residue 128 type MOD_RES sequence T description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 37) chain D residue 252 type MOD_RES sequence L description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 38) chain D residue 353 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 39) chain D residue 367 type MOD_RES sequence L description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 40) chain D residue 410 type MOD_RES sequence F description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 41) chain D residue 419 type MOD_RES sequence R description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 42) chain D residue 495 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI7 43) chain D residue 337 type MOD_RES sequence P description Phosphothreonine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI8 44) chain D residue 413 type MOD_RES sequence L description Phosphoserine => ECO:0000250|UniProtKB:P00352 source Swiss-Prot : SWS_FT_FI9

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