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 |
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 | VAL64 |
A | ASN66 |
A | PRO102 |
A | LEU103 |
A | TYR104 |
A | TRP105 |
A | PHE106 |
A | ASP117 |
A | THR147 |
A | THR148 |
A | GLY149 |
A | GLY150 |
A | TYR155 |
A | GLU193 |
A | GLU197 |
A | ARG200 |
A | VAL204 |
A | STI233 |
A | HOH281 |
A | HOH289 |
A | HOH304 |
A | HOH367 |
A | HOH382 |
A | HOH418 |
A | HIS11 |
A | LYS15 |
A | SER16 |
A | PHE17 |
A | ASN18 |
A | SER20 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE STI A 233 |
Chain | Residue |
A | ASP52 |
A | ILE55 |
A | GLY57 |
A | LEU59 |
A | TRP105 |
A | PHE106 |
A | PHE126 |
A | GLY149 |
A | MET154 |
A | GLY174 |
A | PHE178 |
A | GLU193 |
A | FAD232 |
A | HOH248 |
A | HOH255 |
A | HOH433 |
A | HOH435 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MRD A 234 |
Chain | Residue |
A | TYR75 |
A | ARG92 |
A | GLY123 |
A | PHE124 |
A | LEU137 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MRD A 235 |
Chain | Residue |
A | GLN77 |
A | SER79 |
A | ASP127 |
A | ILE128 |
A | PRO129 |
A | HOH316 |
A | HOH345 |
A | HOH379 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS11 | |
A | PHE17 | |
A | THR147 | |
A | TYR155 | |
A | GLU193 | |
A | ARG200 | |
A | LEU103 | |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | CYS222 | |
A | PHE126 | |
A | HIS173 | |
A | HIS177 | |
Chain | Residue | Details |
A | SER79 | |
A | SER196 | |