4FGJ
Oxidized quinone reductase 2 in complex with primaquine
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 | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 301 |
| Chain | Residue |
| A | HIS173 |
| A | HIS177 |
| A | CYS222 |
| site_id | AC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD A 302 |
| 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 | GLU197 |
| A | ARG200 |
| A | LYS201 |
| A | 1PQ303 |
| A | HOH429 |
| A | HOH485 |
| A | HOH500 |
| A | HOH508 |
| A | HOH545 |
| A | HOH549 |
| A | HOH551 |
| B | ASN66 |
| B | ASP117 |
| A | HIS11 |
| A | LYS15 |
| A | SER16 |
| A | PHE17 |
| A | ASN18 |
| A | SER20 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 1PQ A 303 |
| Chain | Residue |
| A | TRP105 |
| A | PHE106 |
| A | GLY149 |
| A | GLY150 |
| A | MET154 |
| A | ASN161 |
| A | GLU193 |
| A | FAD302 |
| A | HOH593 |
| A | HOH608 |
| A | HOH621 |
| A | HOH652 |
| B | PHE126 |
| B | GLY174 |
| B | PHE178 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 1PQ A 304 |
| Chain | Residue |
| A | GLN122 |
| A | PHE126 |
| A | GLY174 |
| A | PHE178 |
| A | HOH598 |
| A | HOH643 |
| B | TRP105 |
| B | PHE106 |
| B | GLY149 |
| B | GLY150 |
| B | ASN161 |
| B | GLU193 |
| B | FAD303 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 301 |
| Chain | Residue |
| B | LYS76 |
| B | ARG78 |
| B | ASP163 |
| B | ARG165 |
| B | HOH574 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 302 |
| Chain | Residue |
| B | HIS173 |
| B | HIS177 |
| B | CYS222 |
| site_id | AC7 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD B 303 |
| Chain | Residue |
| A | ASN66 |
| A | ASP117 |
| A | 1PQ304 |
| 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 | ARG200 |
| B | HOH451 |
| B | HOH489 |
| B | HOH518 |
| B | HOH527 |
| B | HOH547 |
| B | HOH564 |
| B | HOH598 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 304 |
| Chain | Residue |
| B | ASP54 |
| B | ASP83 |
| B | ARG118 |
| B | HOH528 |
| B | HOH698 |
| B | GLU47 |
| B | LYS53 |
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 |
