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4ZVK

Reduced quinone reductase 2 in complex with ethidium

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 Residues28
Detailsbinding site for residue FAD A 302
ChainResidue
APRO102
ALEU103
ATYR104
ATRP105
APHE106
ATHR147
ATHR148
AGLY149
AGLY150
ATYR155
AGLU193
AGLU197
AARG200
AHOH403
AHOH476
AHOH506
BASN66
BGLY68
BASP117
BET301
BHOH509
BHOH510
AHIS11
ALYS15
ASER16
APHE17
AASN18
ASER20

site_idAC3
Number of Residues11
Detailsbinding site for residue ET A 303
ChainResidue
AGLY68
ATHR71
AGLN122
APHE126
APHE178
AHOH504
AHOH509
BGLU193
BFAD303
BET304
BHOH474

site_idAC4
Number of Residues9
Detailsbinding site for residue ET B 301
ChainResidue
AGLU193
AFAD302
AHOH481
BGLY68
BTHR71
BGLN122
BPHE126
BPHE178
BHOH489

site_idAC5
Number of Residues3
Detailsbinding site for residue ZN B 302
ChainResidue
BHIS173
BHIS177
BCYS222

site_idAC6
Number of Residues30
Detailsbinding site for residue FAD B 303
ChainResidue
AASN66
AGLY68
AASP117
AET303
AHOH485
BHIS11
BLYS15
BSER16
BPHE17
BASN18
BSER20
BPRO102
BLEU103
BTYR104
BTRP105
BPHE106
BTHR147
BTHR148
BGLY149
BGLY150
BTYR155
BGLU193
BGLU197
BARG200
BLYS201
BHOH404
BHOH447
BHOH456
BHOH467
BHOH505

site_idAC7
Number of Residues4
Detailsbinding site for residue ET B 304
ChainResidue
ATHR213
AET303
BMET154
BILE194

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

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PDB entries from 2024-04-24

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