1SG0
Crystal structure analysis of QR2 in complex with resveratrol
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 231 |
| Chain | Residue |
| A | HIS173 |
| A | HIS177 |
| A | CYS222 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 232 |
| Chain | Residue |
| B | HIS173 |
| B | HIS177 |
| B | CYS222 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD B 433 |
| Chain | Residue |
| B | LYS15 |
| B | SER16 |
| B | PHE17 |
| B | ASN18 |
| B | SER20 |
| B | LEU103 |
| B | TYR104 |
| B | TRP105 |
| B | PHE106 |
| B | THR147 |
| B | THR148 |
| B | GLY149 |
| B | GLY150 |
| B | TYR155 |
| B | PRO192 |
| B | GLU193 |
| B | GLU197 |
| B | ARG200 |
| B | HOH559 |
| B | HOH615 |
| B | HOH617 |
| B | HOH623 |
| B | HOH678 |
| A | ASP117 |
| A | STL501 |
| B | HIS11 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FAD A 434 |
| Chain | Residue |
| A | HIS11 |
| A | LYS15 |
| A | SER16 |
| A | PHE17 |
| A | ASN18 |
| A | SER20 |
| A | LEU103 |
| A | TYR104 |
| A | TRP105 |
| A | PHE106 |
| A | THR147 |
| A | THR148 |
| A | GLY149 |
| A | GLY150 |
| A | TYR155 |
| A | PRO192 |
| A | GLU193 |
| A | ARG200 |
| A | LYS201 |
| A | HOH588 |
| A | HOH603 |
| A | HOH613 |
| B | ASP117 |
| B | STL502 |
| B | HOH566 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE STL A 501 |
| Chain | Residue |
| A | GLY68 |
| A | PHE126 |
| A | GLY174 |
| A | PHE178 |
| A | HOH548 |
| A | HOH604 |
| B | TRP105 |
| B | PHE106 |
| B | GLY150 |
| B | ASN161 |
| B | FAD433 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE STL B 502 |
| Chain | Residue |
| A | TRP105 |
| A | PHE106 |
| A | GLY150 |
| A | ASN161 |
| A | FAD434 |
| B | LEU120 |
| B | PHE126 |
| B | GLY174 |
| B | PHE178 |
| B | HOH504 |
| B | HOH531 |
| B | HOH612 |
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 | GLN12 | |
| B | TYR104 | |
| B | THR148 | |
| B | THR156 | |
| B | ILE194 | |
| B | LYS201 | |
| A | ASN18 | |
| A | TYR104 | |
| A | THR148 | |
| A | THR156 | |
| A | ILE194 | |
| A | LYS201 | |
| B | GLN12 | |
| B | ASN18 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP127 | |
| A | GLY174 | |
| A | PHE178 | |
| A | THR223 | |
| B | ASP127 | |
| B | GLY174 | |
| B | PHE178 | |
| B | THR223 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | LEU80 | |
| A | GLU197 | |
| B | LEU80 | |
| B | GLU197 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1d4a |
| Chain | Residue | Details |
| A | TYR155 | |
| A | ASN161 | |
| A | GLY149 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1d4a |
| Chain | Residue | Details |
| B | TYR155 | |
| B | ASN161 | |
| B | GLY149 |
