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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
ChainGOidnamespacecontents
A0000209biological_processprotein polyubiquitination
A0002931biological_processresponse to ischemia
A0003723molecular_functionRNA binding
A0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
A0004128molecular_functioncytochrome-b5 reductase activity, acting on NAD(P)H
A0004784molecular_functionsuperoxide dismutase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006116biological_processNADH oxidation
A0006743biological_processubiquinone metabolic process
A0006801biological_processsuperoxide metabolic process
A0006805biological_processxenobiotic metabolic process
A0006809biological_processnitric oxide biosynthetic process
A0006979biological_processresponse to oxidative stress
A0007271biological_processsynaptic transmission, cholinergic
A0007584biological_processresponse to nutrient
A0008753molecular_functionNADPH dehydrogenase (quinone) activity
A0009410biological_processresponse to xenobiotic stimulus
A0009636biological_processresponse to toxic substance
A0009725biological_processresponse to hormone
A0009743biological_processresponse to carbohydrate
A0010033biological_processresponse to organic substance
A0014070biological_processresponse to organic cyclic compound
A0014075biological_processresponse to amine
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0030163biological_processprotein catabolic process
A0030425cellular_componentdendrite
A0032355biological_processresponse to estradiol
A0032496biological_processresponse to lipopolysaccharide
A0033574biological_processresponse to testosterone
A0034599biological_processcellular response to oxidative stress
A0042177biological_processnegative regulation of protein catabolic process
A0042360biological_processvitamin E metabolic process
A0042373biological_processvitamin K metabolic process
A0042802molecular_functionidentical protein binding
A0043025cellular_componentneuronal cell body
A0043066biological_processnegative regulation of apoptotic process
A0043279biological_processresponse to alkaloid
A0043525biological_processpositive regulation of neuron apoptotic process
A0045087biological_processinnate immune response
A0045202cellular_componentsynapse
A0045454biological_processcell redox homeostasis
A0045471biological_processresponse to ethanol
A0050136molecular_functionNADH:ubiquinone reductase (non-electrogenic) activity
A0051602biological_processresponse to electrical stimulus
A0070301biological_processcellular response to hydrogen peroxide
A0070995biological_processNADPH oxidation
A0071248biological_processcellular response to metal ion
A0110076biological_processnegative regulation of ferroptosis
A1901698biological_processresponse to nitrogen compound
A1904772biological_processresponse to tetrachloromethane
A1904844biological_processresponse to L-glutamine
A1904880biological_processresponse to hydrogen sulfide
A1905395biological_processresponse to flavonoid
Functional Information from PDB Data
site_idAC1
Number of Residues31
DetailsBINDING SITE FOR RESIDUE FAD A 1225
ChainResidue
AHIS12
AGLN105
ATRP106
APHE107
ATHR148
ATHR149
AGLY150
AGLY151
ATYR156
AILE193
AARG201
ATHR16
ALEU205
ADTC1226
AHOH2008
AHOH2013
AHOH2014
AHOH2131
AHOH2132
AHOH2133
AHOH2135
AHOH2136
ASER17
AHOH2137
AHOH2138
APHE18
AASN19
AALA21
AGLN67
APRO103
ALEU104

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE DTC A 1226
ChainResidue
ALYS90
ATRP106
ATYR127
ATYR129
AGLY150
AGLY151
AMET155
ATYR156
AILE161
AHIS162
APHE179
AFAD1225
AHOH2118
AHOH2139

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396
ChainResidueDetails
ALEU104
ATHR148
ATYR156
AARG201
AHIS12
APHE18
AGLN67

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AALA126

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER82

site_idSWS_FT_FI4
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS251
ALYS250

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 3
ChainResidueDetails
AGLY150electrostatic stabiliser, hydrogen bond donor
ATYR156electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
AHIS162hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay

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PDB entries from 2024-06-12

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