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5ENV

YEAST ALCOHOL DEHYDROGENASE WITH BOUND COENZYME

Replaces:  5C1K
Functional Information from GO Data
ChainGOidnamespacecontents
A0000947biological_processamino acid catabolic process to alcohol via Ehrlich pathway
A0004022molecular_functionalcohol dehydrogenase (NAD+) activity
A0004552molecular_functionoctanol dehydrogenase (NAD+) activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0019170molecular_functionmethylglyoxal reductase (NADH) activity
A0019655biological_processpyruvate fermentation to ethanol
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0047655molecular_functionallyl-alcohol dehydrogenase activity
A0120542molecular_functionethanol dehydrogenase (NAD+) activity
A1904408molecular_functionmelatonin binding
A1990362molecular_functionbutanol dehydrogenase (NAD+) activity
B0000947biological_processamino acid catabolic process to alcohol via Ehrlich pathway
B0004022molecular_functionalcohol dehydrogenase (NAD+) activity
B0004552molecular_functionoctanol dehydrogenase (NAD+) activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0008270molecular_functionzinc ion binding
B0016491molecular_functionoxidoreductase activity
B0019170molecular_functionmethylglyoxal reductase (NADH) activity
B0019655biological_processpyruvate fermentation to ethanol
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0047655molecular_functionallyl-alcohol dehydrogenase activity
B0120542molecular_functionethanol dehydrogenase (NAD+) activity
B1904408molecular_functionmelatonin binding
B1990362molecular_functionbutanol dehydrogenase (NAD+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue ZN A 401
ChainResidue
ACYS43
ATHR45
AHIS66
ACYS153
ANAD403
AETF404

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 402
ChainResidue
ACYS111
ACYS97
ACYS100
ACYS103

site_idAC3
Number of Residues25
Detailsbinding site for residue NAD A 403
ChainResidue
AHIS44
ATHR45
AHIS48
ATRP54
ATHR157
ASER176
AGLY177
AALA179
AGLY180
AGLY181
ALEU182
AASP201
ALYS206
APHE221
ASER246
AVAL268
AGLY269
AMET270
ASER293
AVAL295
AARG340
AZN401
AETF404
AHOH508
BVAL284

site_idAC4
Number of Residues9
Detailsbinding site for residue ETF A 404
ChainResidue
ATHR45
ATRP54
AHIS66
ATRP92
ACYS153
AMET270
ATYR294
AZN401
ANAD403

site_idAC5
Number of Residues5
Detailsbinding site for residue ZN B 401
ChainResidue
BCYS43
BHIS66
BGLU67
BCYS153
BETF404

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN B 402
ChainResidue
BCYS97
BCYS100
BCYS103
BCYS111

site_idAC7
Number of Residues20
Detailsbinding site for residue NAD B 403
ChainResidue
AVAL284
BHIS44
BGLY177
BGLY180
BGLY181
BLEU182
BILE200
BASP201
BLYS206
BPHE221
BVAL245
BSER246
BVAL247
BALA251
BVAL268
BMET270
BSER293
BTYR294
BVAL295
BETF404

site_idAC8
Number of Residues7
Detailsbinding site for residue ETF B 404
ChainResidue
BTHR45
BHIS66
BTRP92
BCYS153
BTYR294
BZN401
BNAD403

Functional Information from PROSITE/UniProt
site_idPS00059
Number of Residues15
DetailsADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEgAGVvvgmGenV
ChainResidueDetails
AGLY65-VAL79

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25157460","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26743849","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4W6Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5ENV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26743849","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5ENV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"description":"in the open conformation","evidences":[{"source":"PubMed","id":"25157460","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26743849","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4W6Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5ENV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"320000","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15665377","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues10
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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