5FUQ
CRYSTAL STRUCTURE OF THE H80R VARIANT OF NQO1 BOUND TO DICOUMAROL
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000209 | biological_process | protein polyubiquitination |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| A | 0004128 | molecular_function | cytochrome-b5 reductase activity, acting on NAD(P)H |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006743 | biological_process | ubiquinone metabolic process |
| A | 0006805 | biological_process | xenobiotic metabolic process |
| A | 0006809 | biological_process | nitric oxide biosynthetic process |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0007271 | biological_process | synaptic transmission, cholinergic |
| A | 0008753 | molecular_function | NADPH dehydrogenase (quinone) activity |
| A | 0009636 | biological_process | response to toxic substance |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019430 | biological_process | removal of superoxide radicals |
| A | 0030163 | biological_process | protein catabolic process |
| A | 0032496 | biological_process | response to lipopolysaccharide |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| A | 0042177 | biological_process | negative regulation of protein catabolic process |
| A | 0042360 | biological_process | vitamin E metabolic process |
| A | 0042373 | biological_process | vitamin K metabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0045087 | biological_process | innate immune response |
| A | 0045202 | cellular_component | synapse |
| A | 0045454 | biological_process | cell redox homeostasis |
| A | 0050136 | molecular_function | NADH dehydrogenase (quinone) (non-electrogenic) activity |
| A | 0110076 | biological_process | negative regulation of ferroptosis |
| B | 0000209 | biological_process | protein polyubiquitination |
| B | 0003723 | molecular_function | RNA binding |
| B | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| B | 0004128 | molecular_function | cytochrome-b5 reductase activity, acting on NAD(P)H |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006743 | biological_process | ubiquinone metabolic process |
| B | 0006805 | biological_process | xenobiotic metabolic process |
| B | 0006809 | biological_process | nitric oxide biosynthetic process |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0007271 | biological_process | synaptic transmission, cholinergic |
| B | 0008753 | molecular_function | NADPH dehydrogenase (quinone) activity |
| B | 0009636 | biological_process | response to toxic substance |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019430 | biological_process | removal of superoxide radicals |
| B | 0030163 | biological_process | protein catabolic process |
| B | 0032496 | biological_process | response to lipopolysaccharide |
| B | 0034599 | biological_process | cellular response to oxidative stress |
| B | 0042177 | biological_process | negative regulation of protein catabolic process |
| B | 0042360 | biological_process | vitamin E metabolic process |
| B | 0042373 | biological_process | vitamin K metabolic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0045087 | biological_process | innate immune response |
| B | 0045202 | cellular_component | synapse |
| B | 0045454 | biological_process | cell redox homeostasis |
| B | 0050136 | molecular_function | NADH dehydrogenase (quinone) (non-electrogenic) activity |
| B | 0110076 | biological_process | negative regulation of ferroptosis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD B 1274 |
| Chain | Residue |
| A | GLN67 |
| B | ASN19 |
| B | ALA21 |
| B | PRO103 |
| B | LEU104 |
| B | GLN105 |
| B | TRP106 |
| B | PHE107 |
| B | THR148 |
| B | THR149 |
| B | GLY150 |
| A | TYR68 |
| B | GLY151 |
| B | TYR156 |
| B | ILE193 |
| B | ARG201 |
| B | LEU205 |
| B | DTC1275 |
| B | HOH2012 |
| B | HOH2174 |
| B | HOH2175 |
| B | HOH2176 |
| A | HOH2072 |
| B | HOH2177 |
| B | HOH2178 |
| B | HOH2179 |
| B | HOH2180 |
| A | HOH2075 |
| A | HOH2117 |
| B | HIS12 |
| B | THR16 |
| B | SER17 |
| B | PHE18 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FAD A 1274 |
| Chain | Residue |
| A | HIS12 |
| A | THR16 |
| A | SER17 |
| A | PHE18 |
| A | ASN19 |
| A | ALA21 |
| A | PRO103 |
| A | LEU104 |
| A | GLN105 |
| A | TRP106 |
| A | PHE107 |
| A | THR148 |
| A | THR149 |
| A | GLY150 |
| A | GLY151 |
| A | TYR156 |
| A | ILE193 |
| A | ARG201 |
| A | LEU205 |
| A | DTC1275 |
| A | HOH2209 |
| A | HOH2210 |
| A | HOH2212 |
| B | GLN67 |
| B | PRO69 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DTC B 1275 |
| Chain | Residue |
| A | TYR127 |
| A | TYR129 |
| A | MET132 |
| A | PHE179 |
| A | PHE237 |
| A | DTC1276 |
| A | HOH2122 |
| B | TRP106 |
| B | GLY150 |
| B | GLY151 |
| B | MET155 |
| B | HIS162 |
| B | FAD1274 |
| B | HOH2181 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE DTC A 1275 |
| Chain | Residue |
| A | GLY150 |
| A | GLY151 |
| A | MET155 |
| A | HIS162 |
| A | FAD1274 |
| A | DTC1276 |
| A | HOH2211 |
| B | TYR127 |
| B | TYR129 |
| B | PHE179 |
| B | PHE233 |
| B | PHE237 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE DTC A 1276 |
| Chain | Residue |
| A | TYR129 |
| A | GLY150 |
| A | HIS195 |
| A | DTC1275 |
| A | HOH2214 |
| B | HIS195 |
| B | PHE233 |
| B | GLN234 |
| B | DTC1275 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 1277 |
| Chain | Residue |
| A | THR128 |
| A | TYR129 |
| B | GLN234 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B 1276 |
| Chain | Residue |
| B | SER13 |
| B | HOH2005 |
| B | HOH2088 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 1278 |
| Chain | Residue |
| A | SER13 |
| A | HOH2004 |
| A | HOH2107 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 1277 |
| Chain | Residue |
| B | GLU124 |
| B | TYR127 |
| B | THR128 |
| B | TYR129 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10543876","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10706635","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11735396","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 3 |
| Chain | Residue | Details |
| A | GLY150 | electrostatic stabiliser, hydrogen bond donor |
| A | TYR156 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | HIS162 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 3 |
| Chain | Residue | Details |
| B | GLY150 | electrostatic stabiliser, hydrogen bond donor |
| B | TYR156 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | HIS162 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
