Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1DXQ

CRYSTAL STRUCTURE OF MOUSE NAD[P]H-QUINONE OXIDOREDUCTASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000209biological_processprotein polyubiquitination
A0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
A0004784molecular_functionsuperoxide dismutase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006743biological_processubiquinone metabolic process
A0006801biological_processsuperoxide metabolic process
A0006979biological_processresponse to oxidative stress
A0008753molecular_functionNADPH dehydrogenase (quinone) activity
A0009410biological_processresponse to xenobiotic stimulus
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0030163biological_processprotein catabolic process
A0030425cellular_componentdendrite
A0032496biological_processresponse to lipopolysaccharide
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
A0043086biological_processnegative regulation of catalytic activity
A0043525biological_processpositive regulation of neuron apoptotic process
A0045087biological_processinnate immune response
A0045454biological_processcell redox homeostasis
A0050136molecular_functionNADH dehydrogenase (quinone) (non-electrogenic) activity
A0061771biological_processresponse to caloric restriction
A0070301biological_processcellular response to hydrogen peroxide
A0110076biological_processnegative regulation of ferroptosis
A1902690biological_processpositive regulation of NAD metabolic process
A1904844biological_processresponse to L-glutamine
B0000209biological_processprotein polyubiquitination
B0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
B0004784molecular_functionsuperoxide dismutase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006743biological_processubiquinone metabolic process
B0006801biological_processsuperoxide metabolic process
B0006979biological_processresponse to oxidative stress
B0008753molecular_functionNADPH dehydrogenase (quinone) activity
B0009410biological_processresponse to xenobiotic stimulus
B0016491molecular_functionoxidoreductase activity
B0019430biological_processremoval of superoxide radicals
B0030163biological_processprotein catabolic process
B0030425cellular_componentdendrite
B0032496biological_processresponse to lipopolysaccharide
B0034599biological_processcellular response to oxidative stress
B0042177biological_processnegative regulation of protein catabolic process
B0042360biological_processvitamin E metabolic process
B0042373biological_processvitamin K metabolic process
B0042802molecular_functionidentical protein binding
B0043025cellular_componentneuronal cell body
B0043066biological_processnegative regulation of apoptotic process
B0043086biological_processnegative regulation of catalytic activity
B0043525biological_processpositive regulation of neuron apoptotic process
B0045087biological_processinnate immune response
B0045454biological_processcell redox homeostasis
B0050136molecular_functionNADH dehydrogenase (quinone) (non-electrogenic) activity
B0061771biological_processresponse to caloric restriction
B0070301biological_processcellular response to hydrogen peroxide
B0110076biological_processnegative regulation of ferroptosis
B1902690biological_processpositive regulation of NAD metabolic process
B1904844biological_processresponse to L-glutamine
C0000209biological_processprotein polyubiquitination
C0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
C0004784molecular_functionsuperoxide dismutase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006743biological_processubiquinone metabolic process
C0006801biological_processsuperoxide metabolic process
C0006979biological_processresponse to oxidative stress
C0008753molecular_functionNADPH dehydrogenase (quinone) activity
C0009410biological_processresponse to xenobiotic stimulus
C0016491molecular_functionoxidoreductase activity
C0019430biological_processremoval of superoxide radicals
C0030163biological_processprotein catabolic process
C0030425cellular_componentdendrite
C0032496biological_processresponse to lipopolysaccharide
C0034599biological_processcellular response to oxidative stress
C0042177biological_processnegative regulation of protein catabolic process
C0042360biological_processvitamin E metabolic process
C0042373biological_processvitamin K metabolic process
C0042802molecular_functionidentical protein binding
C0043025cellular_componentneuronal cell body
C0043066biological_processnegative regulation of apoptotic process
C0043086biological_processnegative regulation of catalytic activity
C0043525biological_processpositive regulation of neuron apoptotic process
C0045087biological_processinnate immune response
C0045454biological_processcell redox homeostasis
C0050136molecular_functionNADH dehydrogenase (quinone) (non-electrogenic) activity
C0061771biological_processresponse to caloric restriction
C0070301biological_processcellular response to hydrogen peroxide
C0110076biological_processnegative regulation of ferroptosis
C1902690biological_processpositive regulation of NAD metabolic process
C1904844biological_processresponse to L-glutamine
D0000209biological_processprotein polyubiquitination
D0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
D0004784molecular_functionsuperoxide dismutase activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006743biological_processubiquinone metabolic process
D0006801biological_processsuperoxide metabolic process
D0006979biological_processresponse to oxidative stress
D0008753molecular_functionNADPH dehydrogenase (quinone) activity
D0009410biological_processresponse to xenobiotic stimulus
D0016491molecular_functionoxidoreductase activity
D0019430biological_processremoval of superoxide radicals
D0030163biological_processprotein catabolic process
D0030425cellular_componentdendrite
D0032496biological_processresponse to lipopolysaccharide
D0034599biological_processcellular response to oxidative stress
D0042177biological_processnegative regulation of protein catabolic process
D0042360biological_processvitamin E metabolic process
D0042373biological_processvitamin K metabolic process
D0042802molecular_functionidentical protein binding
D0043025cellular_componentneuronal cell body
D0043066biological_processnegative regulation of apoptotic process
D0043086biological_processnegative regulation of catalytic activity
D0043525biological_processpositive regulation of neuron apoptotic process
D0045087biological_processinnate immune response
D0045454biological_processcell redox homeostasis
D0050136molecular_functionNADH dehydrogenase (quinone) (non-electrogenic) activity
D0061771biological_processresponse to caloric restriction
D0070301biological_processcellular response to hydrogen peroxide
D0110076biological_processnegative regulation of ferroptosis
D1902690biological_processpositive regulation of NAD metabolic process
D1904844biological_processresponse to L-glutamine
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE FAD A 300
ChainResidue
AHIS11
ATRP105
APHE106
ATHR147
ATHR148
AGLY149
AGLY150
ATYR155
AARG200
AMET201
CGLN66
ATHR15
CPRO68
CGLU117
ASER16
APHE17
AASN18
AALA20
APRO102
ALEU103
AGLN104

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE FAD B 300
ChainResidue
ALYS240
BHIS11
BTHR15
BSER16
BPHE17
BASN18
BALA20
BPRO102
BLEU103
BGLN104
BTRP105
BPHE106
BTHR147
BTHR148
BGLY149
BGLY150
BTYR155
BARG200
BMET201
DGLN66
DPRO68
DGLU117

site_idAC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FAD C 300
ChainResidue
AASN64
AGLN66
ATYR67
APRO68
AGLU117
CHIS11
CTHR15
CSER16
CPHE17
CASN18
CALA20
CPRO102
CLEU103
CGLN104
CTRP105
CPHE106
CTHR147
CTHR148
CGLY149
CGLY150
CTYR155
CARG200
CMET201

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE FAD D 300
ChainResidue
BGLN66
BPRO68
BGLU117
DHIS11
DTHR15
DSER16
DPHE17
DASN18
DALA20
DPRO102
DLEU103
DGLN104
DTRP105
DPHE106
DTHR147
DTHR148
DGLY149
DGLY150
DTYR155
DARG200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues196
DetailsRegion: {"description":"Important for apoenzyme conformational stability","evidences":[{"source":"UniProtKB","id":"P15559","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues44
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10706635","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"7527260","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P15559","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P15559","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d4a
ChainResidueDetails
ATYR155
AHIS161
AGLY149

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d4a
ChainResidueDetails
BTYR155
BHIS161
BGLY149

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d4a
ChainResidueDetails
CTYR155
CHIS161
CGLY149

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d4a
ChainResidueDetails
DTYR155
DHIS161
DGLY149

248335

PDB entries from 2026-01-28

PDB statisticsPDBj update infoContact PDBjnumon