eF-site ID 1k02-A PDB Code 1k02 Chain A click to enlarge Title Crystal Structure of Old Yellow Enzyme Mutant Gln114Asn Classification OXIDOREDUCTASE Compound NADPH DEHYDROGENASE 1 Source Saccharomyces pastorianus (Lager yeast) (Saccharomyces carlsbergensis) (OYE1_SACPS) Sequence A:  SFVKDFKPQALGDTNLFKPIKIGNNELLHRAVIPPLTRMR ALHPGNIPNRDWAVEYYTQRAQRPGTMIITEGAFISPQAG GYDNAPGVWSEEQMVEWTKIFNAIHEKKSFVWVNLWVLGW AAFPDNLARDGLRYDSASDNVFMDAEQEAKAKKANNPQHS LTKDEIKQYIKEYVQAAKNSIAAGADGVEIHSANGYLLNQ FLDPHSNTRTDEYGGSIENRARFTLEVVDALVEAIGHEKV GLRLSPYGVFNSMSGGAETGIVAQYAYVAGELEKRAKAGK RLAFVHLVEPRVTNPFLTEGEGEYEGGSNDFVYSIWKGPV IRAGNFALHPEVVREEVKDKRTLIGYGRFFISNPDLVDRL EKGLPLNKYDRDTFYQMSAHGYIDYPTYEEALKLGWDKK Description Functional site 1) chain A residue 380 type sequence H description BINDING SITE FOR RESIDUE MG A 405 source : AC1 2) chain A residue 35 type sequence P description BINDING SITE FOR RESIDUE FMN A 401 source : AC2 3) chain A residue 36 type sequence L description BINDING SITE FOR RESIDUE FMN A 401 source : AC2 4) chain A residue 37 type sequence T description BINDING SITE FOR RESIDUE FMN A 401 source : AC2 5) chain A residue 191 type sequence H description BINDING SITE FOR RESIDUE FMN A 401 source : AC2 6) chain A residue 194 type sequence N description BINDING SITE FOR RESIDUE FMN A 401 source : AC2 7) chain A residue 243 type sequence R description BINDING SITE FOR RESIDUE FMN A 401 source : AC2 8) chain A residue 299 type sequence E description BINDING SITE FOR RESIDUE FMN A 401 source : AC2 9) chain A residue 324 type sequence G description BINDING SITE FOR RESIDUE FMN A 401 source : AC2 10) chain A residue 325 type sequence N description BINDING SITE FOR RESIDUE FMN A 401 source : AC2 11) chain A residue 347 type sequence G description BINDING SITE FOR RESIDUE FMN A 401 source : AC2 12) chain A residue 348 type sequence R description BINDING SITE FOR RESIDUE FMN A 401 source : AC2 13) chain A residue 374 type sequence F description BINDING SITE FOR RESIDUE FMN A 401 source : AC2 14) chain A residue 375 type sequence Y description BINDING SITE FOR RESIDUE FMN A 401 source : AC2 15) chain A residue 38 type catalytic sequence R description 319 source MCSA : MCSA1 16) chain A residue 192 type catalytic sequence S description 319 source MCSA : MCSA1 17) chain A residue 195 type catalytic sequence G description 319 source MCSA : MCSA1 18) chain A residue 197 type catalytic sequence L description 319 source MCSA : MCSA1 19) chain A residue 252 type catalytic sequence S description 319 source MCSA : MCSA1 20) chain A residue 38 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11668181, ECO:0000269|PubMed:7881908, ECO:0000269|PubMed:9830019 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 115 type BINDING sequence L description BINDING => ECO:0000269|PubMed:11668181, ECO:0000269|PubMed:7881908, ECO:0000269|PubMed:9830019 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 244 type BINDING sequence L description BINDING => ECO:0000269|PubMed:11668181, ECO:0000269|PubMed:7881908, ECO:0000269|PubMed:9830019 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 349 type BINDING sequence F description BINDING => ECO:0000269|PubMed:11668181, ECO:0000269|PubMed:7881908, ECO:0000269|PubMed:9830019 source Swiss-Prot : SWS_FT_FI2 24) chain A residue 192 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11668181, ECO:0000269|PubMed:7881908 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 195 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11668181, ECO:0000269|PubMed:7881908 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 376 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:11668181, ECO:0000269|PubMed:7881908 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 197 type ACT_SITE sequence L description Proton donor => ECO:0000305|PubMed:9830020 source Swiss-Prot : SWS_FT_FI1

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