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 | 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
| site_id | SWS_FT_FI1 |
| Number of Residues | 13 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18254726","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19236722","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]} |
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 | |
3FW1
