4QOD
The value crystal structure of apo quinone reductase 2 at 1.35A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001512 | molecular_function | dihydronicotinamide riboside quinone reductase activity |
| A | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016661 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors |
| A | 0031404 | molecular_function | chloride ion binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0071949 | molecular_function | FAD binding |
| A | 1901662 | biological_process | quinone catabolic process |
| A | 1904408 | molecular_function | melatonin binding |
| A | 1905594 | molecular_function | resveratrol binding |
| B | 0001512 | molecular_function | dihydronicotinamide riboside quinone reductase activity |
| B | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016661 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors |
| B | 0031404 | molecular_function | chloride ion binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0071949 | molecular_function | FAD binding |
| B | 1901662 | biological_process | quinone catabolic process |
| B | 1904408 | molecular_function | melatonin binding |
| B | 1905594 | molecular_function | resveratrol binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 301 |
| Chain | Residue |
| A | TRP105 |
| A | HOH421 |
| A | HOH591 |
| B | ASP117 |
| B | LEU120 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 302 |
| Chain | Residue |
| A | PRO192 |
| A | GOL303 |
| A | HOH595 |
| B | ASN66 |
| A | HIS11 |
| A | SER16 |
| A | PHE17 |
| A | ASN18 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 303 |
| Chain | Residue |
| A | SER16 |
| A | PHE17 |
| A | GLU193 |
| A | ARG200 |
| A | GOL302 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 304 |
| Chain | Residue |
| A | TYR67 |
| A | ASP117 |
| A | HOH411 |
| A | HOH527 |
| B | TRP105 |
| B | GOL301 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 305 |
| Chain | Residue |
| A | HIS173 |
| A | HIS177 |
| A | CYS222 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 301 |
| Chain | Residue |
| A | PHE178 |
| A | GOL304 |
| B | LEU103 |
| B | TYR104 |
| B | TRP105 |
| B | HOH410 |
| B | HOH437 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 302 |
| Chain | Residue |
| B | HIS11 |
| B | SER16 |
| B | PHE17 |
| B | ASN18 |
| B | PRO192 |
| B | GLU193 |
| B | HOH433 |
| B | HOH434 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 303 |
| Chain | Residue |
| B | HIS173 |
| B | HIS177 |
| B | CYS222 |
| B | THR223 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722 |
| Chain | Residue | Details |
| A | HIS11 | |
| B | LEU103 | |
| B | THR147 | |
| B | TYR155 | |
| B | GLU193 | |
| B | ARG200 | |
| A | PHE17 | |
| A | LEU103 | |
| A | THR147 | |
| A | TYR155 | |
| A | GLU193 | |
| A | ARG200 | |
| B | HIS11 | |
| B | PHE17 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | PHE126 | |
| A | HIS173 | |
| A | HIS177 | |
| A | CYS222 | |
| B | PHE126 | |
| B | HIS173 | |
| B | HIS177 | |
| B | CYS222 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | SER79 | |
| A | SER196 | |
| B | SER79 | |
| B | SER196 |
