Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1AG8

ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA

Functional Information from GO Data
ChainGOidnamespacecontents
A0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
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
A0018547molecular_functionnitroglycerin reductase activity
A0043878molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity
A0046185biological_processaldehyde catabolic process
A0051287molecular_functionNAD binding
A0106435molecular_functioncarboxylesterase activity
A1903179biological_processregulation of dopamine biosynthetic process
A1905627biological_processregulation of serotonin biosynthetic process
B0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
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
B0018547molecular_functionnitroglycerin reductase activity
B0043878molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity
B0046185biological_processaldehyde catabolic process
B0051287molecular_functionNAD binding
B0106435molecular_functioncarboxylesterase activity
B1903179biological_processregulation of dopamine biosynthetic process
B1905627biological_processregulation of serotonin biosynthetic process
C0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
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
C0018547molecular_functionnitroglycerin reductase activity
C0043878molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity
C0046185biological_processaldehyde catabolic process
C0051287molecular_functionNAD binding
C0106435molecular_functioncarboxylesterase activity
C1903179biological_processregulation of dopamine biosynthetic process
C1905627biological_processregulation of serotonin biosynthetic process
D0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
D0005739cellular_componentmitochondrion
D0005759cellular_componentmitochondrial matrix
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
D0018547molecular_functionnitroglycerin reductase activity
D0043878molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity
D0046185biological_processaldehyde catabolic process
D0051287molecular_functionNAD binding
D0106435molecular_functioncarboxylesterase activity
D1903179biological_processregulation of dopamine biosynthetic process
D1905627biological_processregulation of serotonin biosynthetic process
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
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:9195888
ChainResidueDetails
AGLU268
BGLU268
CGLU268
DGLU268

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:9195888
ChainResidueDetails
ACYS302
BCYS302
CCYS302
DCYS302

site_idSWS_FT_FI3
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z
ChainResidueDetails
AILE166
BGLY245
BGLU268
BGLU399
CILE166
CLYS192
CGLY225
CGLY245
CGLU268
CGLU399
DILE166
ALYS192
DLYS192
DGLY225
DGLY245
DGLU268
DGLU399
AGLY225
AGLY245
AGLU268
AGLU399
BILE166
BLYS192
BGLY225

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Transition state stabilizer => ECO:0000269|PubMed:9195888
ChainResidueDetails
AASN169
BASN169
CASN169
DASN169

site_idSWS_FT_FI5
Number of Residues40
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P47738
ChainResidueDetails
ALYS35
ALYS434
BLYS35
BLYS56
BLYS142
BLYS351
BLYS358
BLYS366
BLYS409
BLYS411
BLYS424
ALYS56
BLYS434
CLYS35
CLYS56
CLYS142
CLYS351
CLYS358
CLYS366
CLYS409
CLYS411
CLYS424
ALYS142
CLYS434
DLYS35
DLYS56
DLYS142
DLYS351
DLYS358
DLYS366
DLYS409
DLYS411
DLYS424
ALYS351
DLYS434
ALYS358
ALYS366
ALYS409
ALYS411
ALYS424

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

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon