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8BB8

Crystal structure of human aldehyde dehydrogenase ALDH3A1 in complex with octanal

Functional Information from GO Data
ChainGOidnamespacecontents
A0004028molecular_function3-chloroallyl aldehyde dehydrogenase activity
A0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
A0004030molecular_functionaldehyde dehydrogenase [NAD(P)+] activity
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006081biological_processcellular aldehyde metabolic process
A0006629biological_processlipid metabolic process
A0006805biological_processxenobiotic metabolic process
A0008106molecular_functionalcohol dehydrogenase (NADP+) activity
A0016020cellular_componentmembrane
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
B0004028molecular_function3-chloroallyl aldehyde dehydrogenase activity
B0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
B0004030molecular_functionaldehyde dehydrogenase [NAD(P)+] activity
B0005515molecular_functionprotein binding
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006081biological_processcellular aldehyde metabolic process
B0006629biological_processlipid metabolic process
B0006805biological_processxenobiotic metabolic process
B0008106molecular_functionalcohol dehydrogenase (NADP+) activity
B0016020cellular_componentmembrane
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
Functional Information from PROSITE/UniProt
site_idPS00070
Number of Residues12
DetailsALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FmNSGQTCVAPD
ChainResidueDetails
APHE236-ASP247

site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP
ChainResidueDetails
ALEU208-PRO215

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:22021038
ChainResidueDetails
AGLU209
ACYS243
BGLU209
BCYS243

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY187
BGLY187

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:22814378
ChainResidueDetails
ASER1
BSER1

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS177
ALYS193
BLYS177
BLYS193

221371

PDB entries from 2024-06-19

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