3TEM
Quinone Oxidoreductase (NQ02) bound to the imidazoacridin-6-one 6a1
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 | 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 | 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 | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 231 |
| Chain | Residue |
| A | HIS173 |
| A | HIS177 |
| A | CYS222 |
| site_id | AC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD A 232 |
| Chain | Residue |
| A | PRO102 |
| A | LEU103 |
| A | TYR104 |
| A | TRP105 |
| A | PHE106 |
| A | THR147 |
| A | THR148 |
| A | GLY149 |
| A | GLY150 |
| A | TYR155 |
| A | GLU193 |
| A | ARG200 |
| A | HOH345 |
| A | HOH350 |
| A | HOH380 |
| A | HOH387 |
| A | HOH402 |
| A | HOH406 |
| A | HOH448 |
| A | HOH507 |
| B | ASN66 |
| B | ASP117 |
| B | HOH343 |
| B | 6A1501 |
| A | HIS11 |
| A | LYS15 |
| A | SER16 |
| A | PHE17 |
| A | ASN18 |
| A | SER20 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 6A1 B 501 |
| Chain | Residue |
| A | TRP105 |
| A | PHE106 |
| A | GLU193 |
| A | FAD232 |
| B | PHE126 |
| B | GLY174 |
| B | PHE178 |
| B | HOH325 |
| B | HOH348 |
| B | HOH352 |
| B | HOH540 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 231 |
| Chain | Residue |
| B | HIS173 |
| B | HIS177 |
| B | CYS222 |
| site_id | AC5 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD B 232 |
| Chain | Residue |
| A | ASN66 |
| A | ASP117 |
| A | 6A1501 |
| A | HOH536 |
| B | HIS11 |
| B | LYS15 |
| B | SER16 |
| B | PHE17 |
| B | ASN18 |
| B | SER20 |
| B | PRO102 |
| B | LEU103 |
| B | TYR104 |
| B | TRP105 |
| B | PHE106 |
| B | THR147 |
| B | THR148 |
| B | GLY149 |
| B | GLY150 |
| B | TYR155 |
| B | GLU193 |
| B | GLU197 |
| B | ARG200 |
| B | HOH307 |
| B | HOH309 |
| B | HOH331 |
| B | HOH332 |
| B | HOH333 |
| B | HOH360 |
| B | HOH448 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 6A1 A 501 |
| Chain | Residue |
| A | PHE126 |
| A | ILE128 |
| A | GLY174 |
| A | PHE178 |
| A | HOH282 |
| A | HOH318 |
| A | HOH351 |
| A | HOH438 |
| B | TRP105 |
| B | PHE106 |
| B | FAD232 |
| B | HOH541 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IMD A 1 |
| Chain | Residue |
| A | ASP52 |
| A | ILE55 |
| A | GLY57 |
| A | GLU218 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18254726","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19236722","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
