3OWH
X-ray Structural study of quinone reductase II inhibition by compounds with micromolar to nanomolar range IC50 values
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 | 28 |
Details | BINDING SITE FOR RESIDUE FAD A 434 |
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 | HOH242 |
A | HOH257 |
A | HOH289 |
B | ASN66 |
B | ASP117 |
B | 52X232 |
B | HOH278 |
B | HOH320 |
A | HIS11 |
A | LYS15 |
A | SER16 |
A | PHE17 |
A | ASN18 |
A | SER20 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE 52X A 232 |
Chain | Residue |
A | GLY68 |
A | GLN122 |
A | PHE126 |
A | PHE131 |
A | PHE178 |
A | HOH251 |
A | HOH277 |
B | GLY149 |
B | GLY150 |
B | MET154 |
B | ASN161 |
B | FAD433 |
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 | 26 |
Details | BINDING SITE FOR RESIDUE FAD B 433 |
Chain | Residue |
A | ASP117 |
A | 52X232 |
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 | HOH311 |
B | HOH354 |
B | HOH362 |
B | HOH371 |
B | HOH373 |
B | HOH392 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 52X B 232 |
Chain | Residue |
A | GLY150 |
A | MET154 |
A | ASN161 |
A | FAD434 |
B | GLY68 |
B | GLN122 |
B | PHE126 |
B | PHE178 |
B | HOH278 |
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 |