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4QOD

The value crystal structure of apo quinone reductase 2 at 1.35A

Functional Information from GO Data
ChainGOidnamespacecontents
A0001512molecular_functiondihydronicotinamide riboside quinone reductase activity
A0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
A0005515molecular_functionprotein binding
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
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 Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
ATRP105
AHOH421
AHOH591
BASP117
BLEU120

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
APRO192
AGOL303
AHOH595
BASN66
AHIS11
ASER16
APHE17
AASN18

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 303
ChainResidue
ASER16
APHE17
AGLU193
AARG200
AGOL302

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 304
ChainResidue
ATYR67
AASP117
AHOH411
AHOH527
BTRP105
BGOL301

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 305
ChainResidue
AHIS173
AHIS177
ACYS222

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 301
ChainResidue
APHE178
AGOL304
BLEU103
BTYR104
BTRP105
BHOH410
BHOH437

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 302
ChainResidue
BHIS11
BSER16
BPHE17
BASN18
BPRO192
BGLU193
BHOH433
BHOH434

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 303
ChainResidue
BHIS173
BHIS177
BCYS222
BTHR223

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues26
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18254726","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19236722","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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