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1A4Z

ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA COMPLEX WITH NAD (REDUCED) AND SAMARIUM (III)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006067biological_processethanol metabolic process
A0006068biological_processethanol catabolic process
A0008957molecular_functionphenylacetaldehyde dehydrogenase (NAD+) activity
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0018937biological_processnitroglycerin metabolic process
A0046185biological_processaldehyde catabolic process
A0051287molecular_functionNAD binding
A0106435molecular_functioncarboxylesterase activity
A0110095biological_processcellular detoxification of aldehyde
A1903179biological_processregulation of dopamine biosynthetic process
A1905627biological_processregulation of serotonin biosynthetic process
B0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006067biological_processethanol metabolic process
B0006068biological_processethanol catabolic process
B0008957molecular_functionphenylacetaldehyde dehydrogenase (NAD+) activity
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0018937biological_processnitroglycerin metabolic process
B0046185biological_processaldehyde catabolic process
B0051287molecular_functionNAD binding
B0106435molecular_functioncarboxylesterase activity
B0110095biological_processcellular detoxification of aldehyde
B1903179biological_processregulation of dopamine biosynthetic process
B1905627biological_processregulation of serotonin biosynthetic process
C0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0006067biological_processethanol metabolic process
C0006068biological_processethanol catabolic process
C0008957molecular_functionphenylacetaldehyde dehydrogenase (NAD+) activity
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0018937biological_processnitroglycerin metabolic process
C0046185biological_processaldehyde catabolic process
C0051287molecular_functionNAD binding
C0106435molecular_functioncarboxylesterase activity
C0110095biological_processcellular detoxification of aldehyde
C1903179biological_processregulation of dopamine biosynthetic process
C1905627biological_processregulation of serotonin biosynthetic process
D0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
D0005739cellular_componentmitochondrion
D0005759cellular_componentmitochondrial matrix
D0006067biological_processethanol metabolic process
D0006068biological_processethanol catabolic process
D0008957molecular_functionphenylacetaldehyde dehydrogenase (NAD+) activity
D0016491molecular_functionoxidoreductase activity
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0018937biological_processnitroglycerin metabolic process
D0046185biological_processaldehyde catabolic process
D0051287molecular_functionNAD binding
D0106435molecular_functioncarboxylesterase activity
D0110095biological_processcellular detoxification of aldehyde
D1903179biological_processregulation of dopamine biosynthetic process
D1905627biological_processregulation of serotonin biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SM A 502
ChainResidue
ANAD501
AHOH514

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SM B 502
ChainResidue
BNAD501
BHOH514

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SM C 502
ChainResidue
CNAD501
CHOH511

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SM D 502
ChainResidue
DNAD501
DHOH512

site_idAC5
Number of Residues28
DetailsBINDING SITE FOR RESIDUE NAD A 501
ChainResidue
AILE166
APRO167
ATRP168
AASN169
AMET174
ALYS192
AGLU195
AGLY225
APRO226
AGLY229
AALA230
APHE243
ATHR244
AGLY245
ASER246
AVAL249
ALEU252
AILE253
AGLU268
AILE269
AGLY270
ACYS302
AGLU399
APHE401
ASM502
AHOH513
AHOH514
AILE165

site_idAC6
Number of Residues26
DetailsBINDING SITE FOR RESIDUE NAD B 501
ChainResidue
BILE165
BILE166
BPRO167
BTRP168
BASN169
BLYS192
BGLU195
BGLY225
BGLY229
BALA230
BPHE243
BTHR244
BGLY245
BSER246
BVAL249
BLEU252
BGLU268
BILE269
BGLY270
BCYS302
BGLU399
BPHE401
BSM502
BHOH513
BHOH514
BHOH517

site_idAC7
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NAD C 501
ChainResidue
CILE165
CILE166
CPRO167
CTRP168
CASN169
CLYS192
CALA194
CGLU195
CGLY225
CPRO226
CGLY229
CALA230
CPHE243
CTHR244
CGLY245
CSER246
CVAL249
CILE253
CGLU268
CILE269
CGLY270
CCYS302
CGLU399
CPHE401
CSM502
CHOH510
CHOH511

site_idAC8
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NAD D 501
ChainResidue
DGLY229
DALA230
DPHE243
DTHR244
DGLY245
DSER246
DVAL249
DILE253
DGLU268
DILE269
DGLY270
DCYS302
DGLU399
DPHE401
DSM502
DHOH511
DHOH512
DILE165
DILE166
DPRO167
DTRP168
DASN169
DLYS192
DALA194
DGLU195
DGLY225
DPRO226

Functional Information from PROSITE/UniProt
site_idPS00070
Number of Residues12
DetailsALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfNQGQCCCAGS
ChainResidueDetails
APHE295-SER306

site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LEIGGKSP
ChainResidueDetails
ALEU267-PRO274

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"9195888","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9195888","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues56
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9195888","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A4Z","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"9195888","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues40
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P47738","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 2025-07-30

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