3WG6
Crystal structure of conjugated polyketone reductase C1 from Candida parapsilosis complexed with NADPH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005575 | cellular_component | cellular_component |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H as acceptor |
| A | 0036441 | molecular_function | 2-dehydropantolactone reductase activity |
| A | 0042180 | biological_process | ketone metabolic process |
| A | 0047011 | molecular_function | 2-dehydropantolactone reductase (A-specific) activity |
| B | 0005575 | cellular_component | cellular_component |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H as acceptor |
| B | 0036441 | molecular_function | 2-dehydropantolactone reductase activity |
| B | 0042180 | biological_process | ketone metabolic process |
| B | 0047011 | molecular_function | 2-dehydropantolactone reductase (A-specific) activity |
| C | 0005575 | cellular_component | cellular_component |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H as acceptor |
| C | 0036441 | molecular_function | 2-dehydropantolactone reductase activity |
| C | 0042180 | biological_process | ketone metabolic process |
| C | 0047011 | molecular_function | 2-dehydropantolactone reductase (A-specific) activity |
| D | 0005575 | cellular_component | cellular_component |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H as acceptor |
| D | 0036441 | molecular_function | 2-dehydropantolactone reductase activity |
| D | 0042180 | biological_process | ketone metabolic process |
| D | 0047011 | molecular_function | 2-dehydropantolactone reductase (A-specific) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NDP A 3001 |
| Chain | Residue |
| A | GLY22 |
| A | SER160 |
| A | ASN161 |
| A | GLN183 |
| A | TYR211 |
| A | GLY212 |
| A | PRO213 |
| A | LEU214 |
| A | THR218 |
| A | ILE256 |
| A | THR257 |
| A | THR23 |
| A | THR258 |
| A | THR259 |
| A | SER260 |
| A | LYS261 |
| A | ARG264 |
| A | PHE296 |
| A | HOH3112 |
| A | HOH3159 |
| A | HOH3188 |
| A | HOH3191 |
| A | GLY24 |
| A | HOH3195 |
| A | THR25 |
| A | LYS26 |
| A | ASP55 |
| A | TYR60 |
| A | LYS85 |
| A | HIS125 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NDP B 3001 |
| Chain | Residue |
| B | GLY22 |
| B | THR23 |
| B | GLY24 |
| B | THR25 |
| B | LYS26 |
| B | ASP55 |
| B | TYR60 |
| B | HIS125 |
| B | SER160 |
| B | ASN161 |
| B | GLN183 |
| B | TYR211 |
| B | GLY212 |
| B | PRO213 |
| B | LEU214 |
| B | ILE217 |
| B | THR218 |
| B | ILE256 |
| B | THR257 |
| B | THR258 |
| B | THR259 |
| B | SER260 |
| B | LYS261 |
| B | ARG264 |
| B | PHE296 |
| B | HOH3129 |
| B | HOH3133 |
| B | HOH3147 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NDP C 3001 |
| Chain | Residue |
| C | GLY22 |
| C | THR23 |
| C | GLY24 |
| C | THR25 |
| C | LYS26 |
| C | ASP55 |
| C | TYR60 |
| C | HIS125 |
| C | SER160 |
| C | ASN161 |
| C | GLN183 |
| C | TYR211 |
| C | GLY212 |
| C | PRO213 |
| C | LEU214 |
| C | ILE217 |
| C | THR218 |
| C | ILE256 |
| C | THR257 |
| C | THR258 |
| C | THR259 |
| C | SER260 |
| C | LYS261 |
| C | ARG264 |
| C | HOH3104 |
| C | HOH3136 |
| C | HOH3168 |
| C | HOH3184 |
| C | HOH3195 |
| site_id | AC4 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NDP D 3001 |
| Chain | Residue |
| D | TYR211 |
| D | GLY212 |
| D | PRO213 |
| D | LEU214 |
| D | ILE217 |
| D | THR218 |
| D | ILE256 |
| D | THR257 |
| D | THR258 |
| D | THR259 |
| D | SER260 |
| D | LYS261 |
| D | ARG264 |
| D | PHE296 |
| D | HOH3113 |
| D | HOH3137 |
| D | HOH3144 |
| D | HOH3165 |
| D | GLY22 |
| D | THR23 |
| D | GLY24 |
| D | THR25 |
| D | LYS26 |
| D | ASP55 |
| D | TYR60 |
| D | LYS85 |
| D | HIS125 |
| D | SER160 |
| D | ASN161 |
| D | GLN183 |
Functional Information from PROSITE/UniProt
| site_id | PS00062 |
| Number of Residues | 18 |
| Details | ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. LerakneglARNIGVSNF |
| Chain | Residue | Details |
| A | LEU145-PHE162 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q76L36","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 48 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23852710","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3WG6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Site: {"description":"Lowers pKa of active site Tyr","evidences":[{"source":"UniProtKB","id":"Q76L36","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
