7BN7
Crystal structure of ene-reductase OYE2 from S. cerevisiae
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003959 | molecular_function | NADPH dehydrogenase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0006915 | biological_process | apoptotic process |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0018548 | molecular_function | pentaerythritol trinitrate reductase activity |
| B | 0003959 | molecular_function | NADPH dehydrogenase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0006915 | biological_process | apoptotic process |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0018548 | molecular_function | pentaerythritol trinitrate reductase activity |
| C | 0003959 | molecular_function | NADPH dehydrogenase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0006915 | biological_process | apoptotic process |
| C | 0010181 | molecular_function | FMN binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0018548 | molecular_function | pentaerythritol trinitrate reductase activity |
| D | 0003959 | molecular_function | NADPH dehydrogenase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0006915 | biological_process | apoptotic process |
| D | 0010181 | molecular_function | FMN binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0018548 | molecular_function | pentaerythritol trinitrate reductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue FMN A 501 |
| Chain | Residue |
| A | PRO35 |
| A | GLY325 |
| A | ASN326 |
| A | GLY348 |
| A | ARG349 |
| A | TYR376 |
| A | GOL502 |
| A | HOH628 |
| A | HOH639 |
| A | HOH677 |
| A | PRO36 |
| A | LEU37 |
| A | THR38 |
| A | GLY73 |
| A | GLN115 |
| A | HIS192 |
| A | ASN195 |
| A | ARG244 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | HIS192 |
| A | ASN195 |
| A | TYR197 |
| A | PHE251 |
| A | PRO296 |
| A | TYR376 |
| A | FMN501 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | binding site for residue FMN B 501 |
| Chain | Residue |
| B | PRO35 |
| B | PRO36 |
| B | LEU37 |
| B | THR38 |
| B | GLY73 |
| B | GLN115 |
| B | HIS192 |
| B | ASN195 |
| B | ARG244 |
| B | GLY325 |
| B | ASN326 |
| B | GLY348 |
| B | ARG349 |
| B | PHE375 |
| B | TYR376 |
| B | GOL502 |
| B | HOH604 |
| B | HOH623 |
| B | HOH643 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| B | ASN195 |
| B | TYR197 |
| B | PHE251 |
| B | PRO296 |
| B | TYR376 |
| B | FMN501 |
| B | HOH643 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | SER309 |
| B | HOH614 |
| D | HOH629 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | binding site for residue FMN C 501 |
| Chain | Residue |
| C | PRO35 |
| C | PRO36 |
| C | LEU37 |
| C | THR38 |
| C | GLY73 |
| C | GLN115 |
| C | HIS192 |
| C | ASN195 |
| C | ARG244 |
| C | GLY325 |
| C | ASN326 |
| C | GLY348 |
| C | ARG349 |
| C | PHE375 |
| C | TYR376 |
| C | GOL502 |
| C | HOH607 |
| C | HOH630 |
| C | HOH638 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 502 |
| Chain | Residue |
| C | TRP117 |
| C | HIS192 |
| C | ASN195 |
| C | TYR197 |
| C | PHE251 |
| C | PRO296 |
| C | FMN501 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | binding site for residue FMN D 501 |
| Chain | Residue |
| D | PRO35 |
| D | PRO36 |
| D | LEU37 |
| D | THR38 |
| D | GLY73 |
| D | GLN115 |
| D | HIS192 |
| D | ASN195 |
| D | ARG244 |
| D | GLY325 |
| D | ASN326 |
| D | GLY348 |
| D | ARG349 |
| D | PHE375 |
| D | GOL502 |
| D | HOH623 |
| D | HOH630 |
| D | HOH659 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue GOL D 502 |
| Chain | Residue |
| D | ASN195 |
| D | TYR197 |
| D | PHE251 |
| D | PRO296 |
| D | TYR376 |
| D | FMN501 |
| D | HIS192 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q02899 |
| Chain | Residue | Details |
| A | TYR197 | |
| B | TYR197 | |
| C | TYR197 | |
| D | TYR197 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q02899 |
| Chain | Residue | Details |
| A | THR38 | |
| A | GLN115 | |
| A | HIS192 | |
| A | ASN195 | |
| A | ARG244 | |
| A | ARG349 | |
| A | TYR376 | |
| B | THR38 | |
| B | GLN115 | |
| B | HIS192 | |
| B | ASN195 | |
| B | ARG244 | |
| B | ARG349 | |
| B | TYR376 | |
| C | THR38 | |
| C | GLN115 | |
| C | HIS192 | |
| C | ASN195 | |
| C | ARG244 | |
| C | ARG349 | |
| C | TYR376 | |
| D | THR38 | |
| D | GLN115 | |
| D | HIS192 | |
| D | ASN195 | |
| D | ARG244 | |
| D | ARG349 | |
| D | TYR376 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | SER353 | |
| B | SER353 | |
| C | SER353 | |
| D | SER353 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
| Chain | Residue | Details |
| A | SER379 | |
| B | SER379 | |
| C | SER379 | |
| D | SER379 |
