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7QK7

Crystal structure of the APO form of ALDH1A3

Functional Information from GO Data
ChainGOidnamespacecontents
A0001758molecular_functionretinal dehydrogenase activity
A0002072biological_processoptic cup morphogenesis involved in camera-type eye development
A0002138biological_processretinoic acid biosynthetic process
A0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
A0004030molecular_functionaldehyde dehydrogenase [NAD(P)+] activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006915biological_processapoptotic process
A0007626biological_processlocomotory behavior
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0021768biological_processnucleus accumbens development
A0031076biological_processembryonic camera-type eye development
A0042472biological_processinner ear morphogenesis
A0042572biological_processretinol metabolic process
A0042573biological_processretinoic acid metabolic process
A0042574biological_processretinal metabolic process
A0042803molecular_functionprotein homodimerization activity
A0043065biological_processpositive regulation of apoptotic process
A0043584biological_processnose development
A0048048biological_processembryonic eye morphogenesis
A0050885biological_processneuromuscular process controlling balance
A0051289biological_processprotein homotetramerization
A0060013biological_processrighting reflex
A0060166biological_processolfactory pit development
A0060324biological_processface development
A0070062cellular_componentextracellular exosome
A0070324molecular_functionthyroid hormone binding
A0070384biological_processHarderian gland development
A0070403molecular_functionNAD+ binding
B0001758molecular_functionretinal dehydrogenase activity
B0002072biological_processoptic cup morphogenesis involved in camera-type eye development
B0002138biological_processretinoic acid biosynthetic process
B0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
B0004030molecular_functionaldehyde dehydrogenase [NAD(P)+] activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0006915biological_processapoptotic process
B0007626biological_processlocomotory behavior
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0021768biological_processnucleus accumbens development
B0031076biological_processembryonic camera-type eye development
B0042472biological_processinner ear morphogenesis
B0042572biological_processretinol metabolic process
B0042573biological_processretinoic acid metabolic process
B0042574biological_processretinal metabolic process
B0042803molecular_functionprotein homodimerization activity
B0043065biological_processpositive regulation of apoptotic process
B0043584biological_processnose development
B0048048biological_processembryonic eye morphogenesis
B0050885biological_processneuromuscular process controlling balance
B0051289biological_processprotein homotetramerization
B0060013biological_processrighting reflex
B0060166biological_processolfactory pit development
B0060324biological_processface development
B0070062cellular_componentextracellular exosome
B0070324molecular_functionthyroid hormone binding
B0070384biological_processHarderian gland development
B0070403molecular_functionNAD+ binding
Functional Information from PROSITE/UniProt
site_idPS00070
Number of Residues12
DetailsALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfNQGQCCTAAS
ChainResidueDetails
APHE307-SER318

site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKNP
ChainResidueDetails
ALEU279-PRO286

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008, ECO:0000305|PubMed:27759097
ChainResidueDetails
AGLU280
BGLU280

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008
ChainResidueDetails
ACYS314
BCYS314

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:27759097, ECO:0007744|PDB:5FHZ
ChainResidueDetails
ALYS204
BGLU411
AGLU207
AGLY257
AGLN361
AGLU411
BLYS204
BGLU207
BGLY257
BGLN361

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASN181
BASN181

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.3, ECO:0007744|PubMed:22814378
ChainResidueDetails
AALA2
BALA2

222036

PDB entries from 2024-07-03

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