Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3TZB

Quinone Oxidoreductase (NQ02) bound to NSC13000

Functional Information from GO Data
ChainGOidnamespacecontents
A0001512molecular_functiondihydronicotinamide riboside quinone reductase activity
A0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0009055molecular_functionelectron transfer activity
A0016491molecular_functionoxidoreductase activity
A0016661molecular_functionoxidoreductase activity, acting on other nitrogenous compounds as donors
A0031404molecular_functionchloride ion binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
A0071949molecular_functionFAD binding
A1901662biological_processquinone catabolic process
A1904408molecular_functionmelatonin binding
A1905594molecular_functionresveratrol binding
B0001512molecular_functiondihydronicotinamide riboside quinone reductase activity
B0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
B0005515molecular_functionprotein binding
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008270molecular_functionzinc ion binding
B0009055molecular_functionelectron transfer activity
B0016491molecular_functionoxidoreductase activity
B0016661molecular_functionoxidoreductase activity, acting on other nitrogenous compounds as donors
B0031404molecular_functionchloride ion binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
B0071949molecular_functionFAD binding
B1901662biological_processquinone catabolic process
B1904408molecular_functionmelatonin binding
B1905594molecular_functionresveratrol binding
C0001512molecular_functiondihydronicotinamide riboside quinone reductase activity
C0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
C0005515molecular_functionprotein binding
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0008270molecular_functionzinc ion binding
C0009055molecular_functionelectron transfer activity
C0016491molecular_functionoxidoreductase activity
C0016661molecular_functionoxidoreductase activity, acting on other nitrogenous compounds as donors
C0031404molecular_functionchloride ion binding
C0042803molecular_functionprotein homodimerization activity
C0046872molecular_functionmetal ion binding
C0070062cellular_componentextracellular exosome
C0071949molecular_functionFAD binding
C1901662biological_processquinone catabolic process
C1904408molecular_functionmelatonin binding
C1905594molecular_functionresveratrol binding
D0001512molecular_functiondihydronicotinamide riboside quinone reductase activity
D0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
D0005515molecular_functionprotein binding
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0008270molecular_functionzinc ion binding
D0009055molecular_functionelectron transfer activity
D0016491molecular_functionoxidoreductase activity
D0016661molecular_functionoxidoreductase activity, acting on other nitrogenous compounds as donors
D0031404molecular_functionchloride ion binding
D0042803molecular_functionprotein homodimerization activity
D0046872molecular_functionmetal ion binding
D0070062cellular_componentextracellular exosome
D0071949molecular_functionFAD binding
D1901662biological_processquinone catabolic process
D1904408molecular_functionmelatonin binding
D1905594molecular_functionresveratrol binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 231
ChainResidue
AHIS173
AHIS177
ACYS222

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FAD A 232
ChainResidue
APRO102
ALEU103
ATYR104
ATRP105
APHE106
ATHR147
ATHR148
AGLY149
AGLY150
ATYR155
AGLU193
AGLU197
AARG200
AHOH266
AHOH373
BASN66
BASP117
BAA501
AHIS11
ALYS15
ASER16
APHE17
AASN18
ASER20

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE AA A 501
ChainResidue
APHE126
APHE178
BTRP105
BFAD232

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 231
ChainResidue
BHIS173
BHIS177
BCYS222

site_idAC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FAD B 232
ChainResidue
AASN66
AASP117
AAA501
BHIS11
BSER16
BPHE17
BASN18
BSER20
BPRO102
BLEU103
BTYR104
BTRP105
BPHE106
BTHR147
BTHR148
BGLY149
BGLY150
BTYR155
BGLU193
BARG200
BVAL204
BHOH250
BHOH286

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE AA B 501
ChainResidue
ATRP105
AFAD232
BPHE126
BPHE178

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN C 231
ChainResidue
CHIS173
CHIS177
CCYS222

site_idAC8
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FAD C 232
ChainResidue
CHIS11
CLYS15
CSER16
CPHE17
CASN18
CSER20
CPRO102
CLEU103
CTYR104
CTRP105
CPHE106
CTHR147
CTHR148
CGLY149
CGLY150
CTYR155
CGLU193
CARG200
CHOH305
CHOH318
CAA501
DASP117
DHOH275

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE AA C 501
ChainResidue
AMET1
CTRP105
CFAD232
DLEU120
DPHE126
DPHE178

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN D 231
ChainResidue
DHIS173
DHIS177
DCYS222

site_idBC2
Number of Residues26
DetailsBINDING SITE FOR RESIDUE FAD D 232
ChainResidue
DHIS11
DLYS15
DSER16
DPHE17
DASN18
DSER20
DPRO102
DLEU103
DTYR104
DTRP105
DPHE106
DTHR147
DTHR148
DGLY149
DGLY150
DTYR155
DGLU193
DGLU197
DARG200
DHOH280
DHOH289
DHOH299
DHOH310
CASN66
CASP117
CAA230

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE AA C 230
ChainResidue
CGLN122
CPHE126
CPHE178
CHOH293
DTRP105
DPHE106
DFAD232

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsBINDING: BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722
ChainResidueDetails
AHIS11
BLEU103
BTHR147
BTYR155
BGLU193
BARG200
CHIS11
CPHE17
CLEU103
CTHR147
CTYR155
APHE17
CGLU193
CARG200
DHIS11
DPHE17
DLEU103
DTHR147
DTYR155
DGLU193
DARG200
ALEU103
ATHR147
ATYR155
AGLU193
AARG200
BHIS11
BPHE17

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING:
ChainResidueDetails
APHE126
CHIS173
CHIS177
CCYS222
DPHE126
DHIS173
DHIS177
DCYS222
AHIS173
AHIS177
ACYS222
BPHE126
BHIS173
BHIS177
BCYS222
CPHE126

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER79
ASER196
BSER79
BSER196
CSER79
CSER196
DSER79
DSER196

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon