4FGL
Reduced quinone reductase 2 in complex with chloroquine
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 |
| C | 0001512 | molecular_function | dihydronicotinamide riboside quinone reductase activity |
| C | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005654 | cellular_component | nucleoplasm |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016661 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors |
| C | 0031404 | molecular_function | chloride ion binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0070062 | cellular_component | extracellular exosome |
| C | 0071949 | molecular_function | FAD binding |
| C | 1901662 | biological_process | quinone catabolic process |
| C | 1904408 | molecular_function | melatonin binding |
| C | 1905594 | molecular_function | resveratrol binding |
| D | 0001512 | molecular_function | dihydronicotinamide riboside quinone reductase activity |
| D | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005654 | cellular_component | nucleoplasm |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016661 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors |
| D | 0031404 | molecular_function | chloride ion binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0070062 | cellular_component | extracellular exosome |
| D | 0071949 | molecular_function | FAD binding |
| D | 1901662 | biological_process | quinone catabolic process |
| D | 1904408 | molecular_function | melatonin binding |
| D | 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 | 33 |
| 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 | CLQ303 |
| A | HOH415 |
| A | HOH430 |
| A | HOH439 |
| A | HOH452 |
| A | HOH453 |
| A | HOH505 |
| A | HOH571 |
| A | HOH657 |
| A | HOH684 |
| B | ASN66 |
| B | ASP117 |
| B | HOH427 |
| A | HIS11 |
| A | LYS15 |
| A | SER16 |
| A | PHE17 |
| A | ASN18 |
| A | SER20 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CLQ A 303 |
| Chain | Residue |
| A | GLY149 |
| A | GLY150 |
| A | ASN161 |
| A | GLU193 |
| A | FAD302 |
| A | HOH415 |
| B | PHE126 |
| B | ILE128 |
| B | PHE178 |
| B | HOH595 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 301 |
| Chain | Residue |
| B | HIS173 |
| B | HIS177 |
| B | CYS222 |
| site_id | AC5 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD B 302 |
| Chain | Residue |
| A | ASP117 |
| A | HOH547 |
| 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 | LYS201 |
| B | CLQ303 |
| B | HOH428 |
| B | HOH439 |
| B | HOH461 |
| B | HOH464 |
| B | HOH475 |
| B | HOH486 |
| B | HOH497 |
| B | HOH561 |
| B | HOH672 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CLQ B 303 |
| Chain | Residue |
| A | GLN122 |
| A | PHE126 |
| A | PHE178 |
| B | GLY150 |
| B | ASN161 |
| B | GLU193 |
| B | FAD302 |
| B | HOH478 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN C 301 |
| Chain | Residue |
| C | HIS173 |
| C | HIS177 |
| C | CYS222 |
| site_id | AC8 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD C 302 |
| Chain | Residue |
| C | TYR104 |
| C | TRP105 |
| C | PHE106 |
| C | THR147 |
| C | THR148 |
| C | GLY149 |
| C | GLY150 |
| C | TYR155 |
| C | GLU193 |
| C | ARG200 |
| C | LYS201 |
| C | CLQ303 |
| C | HOH439 |
| C | HOH451 |
| C | HOH458 |
| C | HOH488 |
| C | HOH490 |
| C | HOH573 |
| C | HOH605 |
| D | ASP117 |
| C | HIS11 |
| C | LYS15 |
| C | SER16 |
| C | PHE17 |
| C | ASN18 |
| C | SER20 |
| C | PRO102 |
| C | LEU103 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CLQ C 303 |
| Chain | Residue |
| C | GLU73 |
| C | GLY149 |
| C | GLY150 |
| C | MET154 |
| C | FAD302 |
| C | HOH451 |
| C | HOH484 |
| C | HOH557 |
| D | GLN122 |
| D | PHE126 |
| D | ILE128 |
| D | PHE178 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN D 301 |
| Chain | Residue |
| D | HIS173 |
| D | HIS177 |
| D | CYS222 |
| site_id | BC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD D 302 |
| Chain | Residue |
| C | ASP117 |
| D | HIS11 |
| D | LYS15 |
| D | SER16 |
| D | PHE17 |
| D | ASN18 |
| D | SER20 |
| D | PRO102 |
| D | LEU103 |
| D | TYR104 |
| D | TRP105 |
| D | PHE106 |
| D | THR147 |
| D | THR148 |
| D | GLY149 |
| D | GLY150 |
| D | TYR155 |
| D | GLU193 |
| D | ARG200 |
| D | LYS201 |
| D | CLQ303 |
| D | HOH407 |
| D | HOH429 |
| D | HOH472 |
| D | HOH489 |
| D | HOH507 |
| D | HOH510 |
| D | HOH566 |
| site_id | BC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CLQ D 303 |
| Chain | Residue |
| C | GLN122 |
| C | PHE126 |
| C | ILE128 |
| C | PHE178 |
| C | HOH639 |
| D | GLY149 |
| D | GLY150 |
| D | MET154 |
| D | GLU193 |
| D | FAD302 |
| D | HOH413 |
| D | HOH479 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CLQ D 304 |
| Chain | Residue |
| D | LYS22 |
| D | ASN23 |
| D | VAL26 |
| D | ASP27 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| 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 | |
| C | HIS11 | |
| C | PHE17 | |
| C | LEU103 | |
| C | THR147 | |
| C | TYR155 | |
| A | PHE17 | |
| C | GLU193 | |
| C | ARG200 | |
| D | HIS11 | |
| D | PHE17 | |
| D | LEU103 | |
| D | THR147 | |
| D | TYR155 | |
| D | GLU193 | |
| D | ARG200 | |
| A | LEU103 | |
| A | THR147 | |
| A | TYR155 | |
| A | GLU193 | |
| A | ARG200 | |
| B | HIS11 | |
| B | PHE17 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | PHE126 | |
| C | HIS173 | |
| C | HIS177 | |
| C | CYS222 | |
| D | PHE126 | |
| D | HIS173 | |
| D | HIS177 | |
| D | CYS222 | |
| A | HIS173 | |
| A | HIS177 | |
| A | CYS222 | |
| B | PHE126 | |
| B | HIS173 | |
| B | HIS177 | |
| B | CYS222 | |
| C | PHE126 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | SER79 | |
| A | SER196 | |
| B | SER79 | |
| B | SER196 | |
| C | SER79 | |
| C | SER196 | |
| D | SER79 | |
| D | SER196 |
