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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
A0006116biological_processNADH oxidation
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0019170molecular_functionmethylglyoxal reductase (NADH) activity
A0019655biological_processglycolytic fermentation to ethanol
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0047655molecular_functionallyl-alcohol dehydrogenase 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
B0006116biological_processNADH oxidation
B0008270molecular_functionzinc ion binding
B0016491molecular_functionoxidoreductase activity
B0019170molecular_functionmethylglyoxal reductase (NADH) activity
B0019655biological_processglycolytic fermentation to ethanol
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0047655molecular_functionallyl-alcohol dehydrogenase 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: BINDING => ECO:0000269|PubMed:25157460, ECO:0000269|PubMed:26743849, ECO:0007744|PDB:4W6Z, ECO:0007744|PDB:5ENV
ChainResidueDetails
ACYS43
BCYS97
BCYS100
BCYS103
BCYS111
BCYS153
AHIS66
ACYS97
ACYS100
ACYS103
ACYS111
ACYS153
BCYS43
BHIS66

site_idSWS_FT_FI2
Number of Residues28
DetailsBINDING: BINDING => ECO:0000269|PubMed:26743849, ECO:0007744|PDB:5ENV
ChainResidueDetails
AHIS44
AVAL268
AMET270
ASER293
AVAL295
AARG340
BHIS44
BTHR45
BHIS48
BGLY180
BGLY181
ATHR45
BLEU182
BASP201
BLYS206
BPHE221
BVAL268
BMET270
BSER293
BVAL295
BARG340
AHIS48
AGLY180
AGLY181
ALEU182
AASP201
ALYS206
APHE221

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: in the open conformation => ECO:0000269|PubMed:25157460, ECO:0000269|PubMed:26743849, ECO:0007744|PDB:4W6Z, ECO:0007744|PDB:5ENV
ChainResidueDetails
AGLU67
BGLU67

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:320000
ChainResidueDetails
ASER1
BSER1

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358
ChainResidueDetails
ASER212
BSER212

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17287358
ChainResidueDetails
ATHR222
BTHR222

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER278
BSER278

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER315
BSER315

site_idSWS_FT_FI9
Number of Residues10
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS225
BLYS318
ALYS233
ALYS286
ALYS318
BLYS225
BLYS233
BLYS286

219140

PDB entries from 2024-05-01

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