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4RQU

Alcohol Dehydrogenase crystal structure in complex with NAD

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001666biological_processresponse to hypoxia
A0004022molecular_functionalcohol dehydrogenase (NAD+) activity
A0005737cellular_componentcytoplasm
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006970biological_processresponse to osmotic stress
A0008270molecular_functionzinc ion binding
A0009409biological_processresponse to cold
A0009413biological_processresponse to flooding
A0009414biological_processresponse to water deprivation
A0009651biological_processresponse to salt stress
A0009737biological_processresponse to abscisic acid
A0009744biological_processresponse to sucrose
A0016491molecular_functionoxidoreductase activity
A0031000biological_processresponse to caffeine
A0032355biological_processresponse to estradiol
A0042542biological_processresponse to hydrogen peroxide
A0042803molecular_functionprotein homodimerization activity
A0046294biological_processformaldehyde catabolic process
A0046872molecular_functionmetal ion binding
A0051903molecular_functionS-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity
A0071456biological_processcellular response to hypoxia
A0120542molecular_functionethanol dehydrogenase (NAD+) activity
A1900039biological_processpositive regulation of cellular response to hypoxia
B0000166molecular_functionnucleotide binding
B0001666biological_processresponse to hypoxia
B0004022molecular_functionalcohol dehydrogenase (NAD+) activity
B0005737cellular_componentcytoplasm
B0005794cellular_componentGolgi apparatus
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006970biological_processresponse to osmotic stress
B0008270molecular_functionzinc ion binding
B0009409biological_processresponse to cold
B0009413biological_processresponse to flooding
B0009414biological_processresponse to water deprivation
B0009651biological_processresponse to salt stress
B0009737biological_processresponse to abscisic acid
B0009744biological_processresponse to sucrose
B0016491molecular_functionoxidoreductase activity
B0031000biological_processresponse to caffeine
B0032355biological_processresponse to estradiol
B0042542biological_processresponse to hydrogen peroxide
B0042803molecular_functionprotein homodimerization activity
B0046294biological_processformaldehyde catabolic process
B0046872molecular_functionmetal ion binding
B0051903molecular_functionS-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity
B0071456biological_processcellular response to hypoxia
B0120542molecular_functionethanol dehydrogenase (NAD+) activity
B1900039biological_processpositive regulation of cellular response to hypoxia
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 400
ChainResidue
ACYS99
ACYS102
ACYS105
ACYS113

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
ACYS47
AHIS69
ACYS177

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 401
ChainResidue
BCYS105
BCYS113
BCYS99
BCYS102

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 402
ChainResidue
BCYS47
BTHR49
BHIS69
BCYS177
BNAD403
BHOH506

site_idAC5
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAD B 403
ChainResidue
BHIS48
BTHR49
BPHE95
BCYS177
BTHR181
BGLY202
BGLY204
BALA205
BVAL206
BASP226
BPHE227
BASN228
BARG231
BCYS271
BTHR272
BVAL295
BVAL297
BPHE322
BARG372
BZN402
BHOH502

Functional Information from PROSITE/UniProt
site_idPS00059
Number of Residues15
DetailsADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEaGGIvesvGegV
ChainResidueDetails
AGLY68-VAL82

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25447145","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38308388","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4RQT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RQU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8CON","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25447145","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4RQU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25447145","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38308388","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4RQU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8CON","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"38308388","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8CON","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18433157","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19245862","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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