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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1BXS

SHEEP LIVER CLASS 1 ALDEHYDE DEHYDROGENASE WITH NAD BOUND

Functional Information from GO Data
ChainGOidnamespacecontents
A0001523biological_processretinoid metabolic process
A0001758molecular_functionretinal dehydrogenase (NAD+) activity
A0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
A0004030molecular_functionaldehyde dehydrogenase [NAD(P)+] activity
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0009449biological_processgamma-aminobutyric acid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0018479molecular_functionbenzaldehyde dehydrogenase (NAD+) activity
A0019145molecular_functionaminobutyraldehyde dehydrogenase (NAD+) activity
A0030392biological_processfructosamine catabolic process
A0030424cellular_componentaxon
A0036438biological_processmaintenance of lens transparency
A0042572biological_processretinol metabolic process
A0045202cellular_componentsynapse
A0051287molecular_functionNAD binding
A0106373molecular_function3-deoxyglucosone dehydrogenase activity
A0110095biological_processcellular detoxification of aldehyde
A0140087molecular_functionacetaldehyde dehydrogenase (NAD+) activity
B0001523biological_processretinoid metabolic process
B0001758molecular_functionretinal dehydrogenase (NAD+) activity
B0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
B0004030molecular_functionaldehyde dehydrogenase [NAD(P)+] activity
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0009449biological_processgamma-aminobutyric acid biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0018479molecular_functionbenzaldehyde dehydrogenase (NAD+) activity
B0019145molecular_functionaminobutyraldehyde dehydrogenase (NAD+) activity
B0030392biological_processfructosamine catabolic process
B0030424cellular_componentaxon
B0036438biological_processmaintenance of lens transparency
B0042572biological_processretinol metabolic process
B0045202cellular_componentsynapse
B0051287molecular_functionNAD binding
B0106373molecular_function3-deoxyglucosone dehydrogenase activity
B0110095biological_processcellular detoxification of aldehyde
B0140087molecular_functionacetaldehyde dehydrogenase (NAD+) activity
C0001523biological_processretinoid metabolic process
C0001758molecular_functionretinal dehydrogenase (NAD+) activity
C0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
C0004030molecular_functionaldehyde dehydrogenase [NAD(P)+] activity
C0005829cellular_componentcytosol
C0006629biological_processlipid metabolic process
C0009449biological_processgamma-aminobutyric acid biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0018479molecular_functionbenzaldehyde dehydrogenase (NAD+) activity
C0019145molecular_functionaminobutyraldehyde dehydrogenase (NAD+) activity
C0030392biological_processfructosamine catabolic process
C0030424cellular_componentaxon
C0036438biological_processmaintenance of lens transparency
C0042572biological_processretinol metabolic process
C0045202cellular_componentsynapse
C0051287molecular_functionNAD binding
C0106373molecular_function3-deoxyglucosone dehydrogenase activity
C0110095biological_processcellular detoxification of aldehyde
C0140087molecular_functionacetaldehyde dehydrogenase (NAD+) activity
D0001523biological_processretinoid metabolic process
D0001758molecular_functionretinal dehydrogenase (NAD+) activity
D0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
D0004030molecular_functionaldehyde dehydrogenase [NAD(P)+] activity
D0005829cellular_componentcytosol
D0006629biological_processlipid metabolic process
D0009449biological_processgamma-aminobutyric acid biosynthetic process
D0016491molecular_functionoxidoreductase activity
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0018479molecular_functionbenzaldehyde dehydrogenase (NAD+) activity
D0019145molecular_functionaminobutyraldehyde dehydrogenase (NAD+) activity
D0030392biological_processfructosamine catabolic process
D0030424cellular_componentaxon
D0036438biological_processmaintenance of lens transparency
D0042572biological_processretinol metabolic process
D0045202cellular_componentsynapse
D0051287molecular_functionNAD binding
D0106373molecular_function3-deoxyglucosone dehydrogenase activity
D0110095biological_processcellular detoxification of aldehyde
D0140087molecular_functionacetaldehyde dehydrogenase (NAD+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAD A 550
ChainResidue
AILE165
APRO226
AGLY229
AALA230
APHE243
AGLY245
ASER246
AVAL249
AILE253
ALEU269
AGLY270
AILE166
ACYS302
AGLN349
ALYS352
AGLU399
APHE401
APRO167
ATRP168
AASN169
ALYS192
AALA194
AGLU195
AGLY225
site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAD B 550
ChainResidue
BILE165
BILE166
BPRO167
BTRP168
BASN169
BLYS192
BALA194
BGLU195
BGLY225
BPRO226
BGLY229
BALA230
BPHE243
BGLY245
BSER246
BVAL249
BILE253
BLEU269
BGLY270
BCYS302
BGLN349
BLYS352
BGLU399
BPHE401
site_idAC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE NAD C 550
ChainResidue
CILE165
CILE166
CPRO167
CTRP168
CASN169
CLYS192
CALA194
CGLU195
CGLY225
CGLY229
CALA230
CPHE243
CGLY245
CSER246
CVAL249
CILE253
CLEU269
CGLY270
CCYS302
CGLN349
CLYS352
CGLU399
CPHE401
site_idAC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAD D 550
ChainResidue
DILE165
DILE166
DPRO167
DTRP168
DASN169
DLYS192
DALA194
DGLU195
DGLY225
DPRO226
DGLY229
DALA230
DPHE243
DGLY245
DSER246
DVAL249
DILE253
DLEU269
DGLY270
DCYS302
DGLN349
DLYS352
DGLU399
DPHE401
Functional Information from PROSITE/UniProt
site_idPS00070
Number of Residues12
DetailsALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FyHQGQCCIAAS
ChainResidueDetails
APHE295-SER306
site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP
ChainResidueDetails
ALEU267-PRO274
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues660
DetailsRegion: {"description":"Mediates interaction with PRMT3","evidences":[{"source":"UniProtKB","id":"P00352","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9862807","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues56
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26373694","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9862807","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BXS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AC0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26373694","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5AC0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P20000","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues32
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P00352","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P00352","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00352","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a4s
ChainResidueDetails
ACYS302
AGLU268
AASN169
site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a4s
ChainResidueDetails
BCYS302
BGLU268
BASN169
site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a4s
ChainResidueDetails
CCYS302
CGLU268
CASN169
site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a4s
ChainResidueDetails
DCYS302
DGLU268
DASN169
site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a4s
ChainResidueDetails
ACYS302
ALYS192
AGLU268
AGLU399
site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a4s
ChainResidueDetails
BCYS302
BLYS192
BGLU268
BGLU399
site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a4s
ChainResidueDetails
CCYS302
CLYS192
CGLU268
CGLU399
site_idCSA8
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a4s
ChainResidueDetails
DCYS302
DLYS192
DGLU268
DGLU399

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PDB entries from 2026-01-14

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