4CET
Crystal structure of the complex of the P187S variant of human NAD(P) H:quinone oxidoreductase with dicoumarol at 2.2 A resolution
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 | 0061771 | biological_process | response to caloric restriction |
| A | 0110076 | biological_process | negative regulation of ferroptosis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD A 1225 |
| Chain | Residue |
| A | HIS12 |
| A | GLN105 |
| A | TRP106 |
| A | PHE107 |
| A | THR148 |
| A | THR149 |
| A | GLY150 |
| A | GLY151 |
| A | TYR156 |
| A | ILE193 |
| A | ARG201 |
| A | THR16 |
| A | LEU205 |
| A | DTC1226 |
| A | HOH2008 |
| A | HOH2013 |
| A | HOH2014 |
| A | HOH2131 |
| A | HOH2132 |
| A | HOH2133 |
| A | HOH2135 |
| A | HOH2136 |
| A | SER17 |
| A | HOH2137 |
| A | HOH2138 |
| A | PHE18 |
| A | ASN19 |
| A | ALA21 |
| A | GLN67 |
| A | PRO103 |
| A | LEU104 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DTC A 1226 |
| Chain | Residue |
| A | LYS90 |
| A | TRP106 |
| A | TYR127 |
| A | TYR129 |
| A | GLY150 |
| A | GLY151 |
| A | MET155 |
| A | TYR156 |
| A | ILE161 |
| A | HIS162 |
| A | PHE179 |
| A | FAD1225 |
| A | HOH2118 |
| A | HOH2139 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396 |
| Chain | Residue | Details |
| A | HIS12 | |
| A | PHE18 | |
| A | GLN67 | |
| A | LEU104 | |
| A | THR148 | |
| A | TYR156 | |
| A | ARG201 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ALA126 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER82 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| A | LYS250 | |
| A | LYS251 |
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 |
