4O0L
Crystal structure of NADPH-Dependent 3-Quinuclidinone Reductase from Rhodotorula Rubra
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0044281 | biological_process | small molecule metabolic process |
| A | 0050085 | molecular_function | mannitol 2-dehydrogenase (NADP+) activity |
| A | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0044281 | biological_process | small molecule metabolic process |
| B | 0050085 | molecular_function | mannitol 2-dehydrogenase (NADP+) activity |
| B | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0044281 | biological_process | small molecule metabolic process |
| C | 0050085 | molecular_function | mannitol 2-dehydrogenase (NADP+) activity |
| C | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0044281 | biological_process | small molecule metabolic process |
| D | 0050085 | molecular_function | mannitol 2-dehydrogenase (NADP+) activity |
| D | 0050664 | molecular_function | oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NDP A 300 |
| Chain | Residue |
| A | GLY35 |
| A | VAL87 |
| A | ASN113 |
| A | ALA114 |
| A | GLY115 |
| A | VAL137 |
| A | THR164 |
| A | THR165 |
| A | SER166 |
| A | TYR181 |
| A | LYS185 |
| A | GLY38 |
| A | PRO210 |
| A | GLY211 |
| A | PHE212 |
| A | PHE213 |
| A | THR215 |
| A | PRO216 |
| A | MET217 |
| A | GLY218 |
| A | HOH413 |
| A | HOH433 |
| A | GLY39 |
| A | HOH441 |
| A | HOH446 |
| A | HOH466 |
| A | ILE40 |
| A | ARG60 |
| A | SER61 |
| A | ALA62 |
| A | CYS85 |
| A | GLU86 |
| site_id | AC2 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NDP B 300 |
| Chain | Residue |
| B | GLY35 |
| B | GLY38 |
| B | GLY39 |
| B | ILE40 |
| B | ARG60 |
| B | SER61 |
| B | ALA62 |
| B | CYS85 |
| B | GLU86 |
| B | VAL87 |
| B | ASN113 |
| B | ALA114 |
| B | GLY115 |
| B | VAL137 |
| B | THR164 |
| B | THR165 |
| B | SER166 |
| B | TYR181 |
| B | LYS185 |
| B | PRO210 |
| B | GLY211 |
| B | PHE212 |
| B | PHE213 |
| B | THR215 |
| B | PRO216 |
| B | MET217 |
| B | GLY218 |
| B | HOH405 |
| B | HOH408 |
| B | HOH424 |
| B | HOH435 |
| B | HOH438 |
| B | HOH465 |
| site_id | AC3 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NDP C 300 |
| Chain | Residue |
| C | GLY35 |
| C | GLY38 |
| C | GLY39 |
| C | ILE40 |
| C | ARG60 |
| C | SER61 |
| C | ALA62 |
| C | CYS85 |
| C | GLU86 |
| C | VAL87 |
| C | ASN113 |
| C | ALA114 |
| C | GLY115 |
| C | VAL137 |
| C | THR164 |
| C | THR165 |
| C | SER166 |
| C | TYR181 |
| C | LYS185 |
| C | PRO210 |
| C | GLY211 |
| C | PHE212 |
| C | PHE213 |
| C | THR215 |
| C | PRO216 |
| C | MET217 |
| C | GLY218 |
| C | HOH401 |
| C | HOH402 |
| C | HOH462 |
| C | HOH463 |
| C | HOH464 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NDP D 300 |
| Chain | Residue |
| D | GLY39 |
| D | ILE40 |
| D | ARG60 |
| D | SER61 |
| D | ALA62 |
| D | CYS85 |
| D | GLU86 |
| D | VAL87 |
| D | ASN113 |
| D | ALA114 |
| D | GLY115 |
| D | VAL137 |
| D | THR164 |
| D | THR165 |
| D | SER166 |
| D | TYR181 |
| D | LYS185 |
| D | PRO210 |
| D | GLY211 |
| D | PHE212 |
| D | PHE213 |
| D | THR215 |
| D | PRO216 |
| D | MET217 |
| D | GLY218 |
| D | HOH410 |
| D | HOH426 |
| D | HOH435 |
| D | HOH463 |
| D | GLY35 |
| D | GLY38 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SarivnvpydQpaYNSSKAAVvHFCrSLA |
| Chain | Residue | Details |
| A | SER168-ALA196 |
