7JWT

Crystal structure of human ALDH1A1 bound to compound (R)-28

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0001523	biological_process	retinoid metabolic process
A	0001758	molecular_function	retinal dehydrogenase activity
A	0004029	molecular_function	aldehyde dehydrogenase (NAD+) activity
A	0005096	molecular_function	GTPase activator activity
A	0005497	molecular_function	androgen binding
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006081	biological_process	cellular aldehyde metabolic process
A	0006629	biological_process	lipid metabolic process
A	0009449	biological_process	gamma-aminobutyric acid biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A	0018479	molecular_function	benzaldehyde dehydrogenase (NAD+) activity
A	0019145	molecular_function	aminobutyraldehyde dehydrogenase (NAD+) activity
A	0030392	biological_process	fructosamine catabolic process
A	0030424	cellular_component	axon
A	0036438	biological_process	maintenance of lens transparency
A	0042572	biological_process	retinol metabolic process
A	0042995	cellular_component	cell projection
A	0045202	cellular_component	synapse
A	0051287	molecular_function	NAD binding
A	0070062	cellular_component	extracellular exosome
A	0106373	molecular_function	3-deoxyglucosone dehydrogenase activity
A	0110095	biological_process	cellular detoxification of aldehyde
A	0120163	biological_process	negative regulation of cold-induced thermogenesis

Functional Information from PROSITE/UniProt

site_id	PS00070
Number of Residues	12
Details	ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FyHQGQCCIAAS

Chain	Residue	Details
A	PHE296-SER307

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site_id	PS00687
Number of Residues	8
Details	ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP

Chain	Residue	Details
A	LEU268-PRO275

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008, ECO:0000269|PubMed:3676276

Chain	Residue	Details
A	GLU269

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008, ECO:0000269|PubMed:3676276

Chain	Residue	Details
A	CYS303

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site_id	SWS_FT_FI3
Number of Residues	7
Details	BINDING: BINDING => ECO:0000269|PubMed:25450233, ECO:0000269|PubMed:25634381, ECO:0007744|PDB:4WB9, ECO:0007744|PDB:4X4L

Chain	Residue	Details
A	ILE167
A	LYS193
A	GLY226
A	GLY246
A	GLU269
A	GLU349
A	GLU400

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site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P20000

Chain	Residue	Details
A	ASN170

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N-acetylserine => ECO:0000269|PubMed:6723659, ECO:0007744|PubMed:22223895

Chain	Residue	Details
A	SER2

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site_id	SWS_FT_FI6
Number of Residues	9
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS91
A	LYS128
A	LYS252
A	LYS353
A	LYS367
A	LYS410
A	LYS419
A	LYS435
A	LYS495

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	THR337

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER413

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