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4U7G

Oxidized quinone reductase 2 in complex with CK2 inhibitor TBBz

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
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS173
AHIS177
ACYS222

site_idAC2
Number of Residues27
Detailsbinding site for residue FAD A 302
ChainResidue
APRO102
ALEU103
ATYR104
ATRP105
APHE106
ATHR147
ATHR148
AGLY149
AGLY150
ATYR155
AGLU193
AARG200
ALYS201
AK17303
AHOH475
AHOH503
AHOH535
AHOH555
BASN66
BASP117
BHOH506
AHIS11
ALYS15
ASER16
APHE17
AASN18
ASER20

site_idAC3
Number of Residues11
Detailsbinding site for residue K17 A 303
ChainResidue
ATRP105
APHE106
AGLY150
AMET154
AASN161
AFAD302
AHOH514
AHOH541
BPHE126
BGLY174
BPHE178

site_idAC4
Number of Residues3
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS173
BHIS177
BCYS222

site_idAC5
Number of Residues27
Detailsbinding site for residue FAD B 302
ChainResidue
AASN66
AASP117
BHIS11
BLYS15
BSER16
BPHE17
BASN18
BSER20
BPRO102
BLEU103
BTYR104
BTRP105
BPHE106
BTHR147
BTHR148
BGLY149
BGLY150
BTYR155
BGLU193
BARG200
BK17303
BHOH499
BHOH550
BHOH582
BHOH583
BHOH588
BHOH590

site_idAC6
Number of Residues9
Detailsbinding site for residue K17 B 303
ChainResidue
APHE126
AGLY174
APHE178
BTRP105
BPHE106
BGLY150
BMET154
BASN161
BFAD302

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:18254726, ECO:0000269|PubMed:19236722
ChainResidueDetails
AHIS11
BLEU103
BTHR147
BTYR155
BGLU193
BARG200
APHE17
ALEU103
ATHR147
ATYR155
AGLU193
AARG200
BHIS11
BPHE17

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
APHE126
AHIS173
AHIS177
ACYS222
BPHE126
BHIS173
BHIS177
BCYS222

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER79
ASER196
BSER79
BSER196

218853

PDB entries from 2024-04-24

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