6DUM

ALDH1A1 N121S in complex with 6-{[(3-fluorophenyl)methyl]sulfanyl}-2-(oxetan-3-yl)-5-phenyl-2,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one (compound 13g)

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 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	0043878	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity
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 PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue YB A 601

Chain	Residue
A	HOH747
A	HOH815
A	HOH825
A	HOH838
A	HOH851
A	HOH858
A	HOH858
A	HOH866

---

site_id	AC2
Number of Residues	8
Details	binding site for residue YB A 602

Chain	Residue
A	CL605
A	CL610
A	CL611
A	HOH701
A	HOH780
A	HOH842
A	HOH859
A	NAI604

---

site_id	AC3
Number of Residues	11
Details	binding site for residue A5Y A 603

Chain	Residue
A	GLY125
A	THR129
A	PHE171
A	MET175
A	TRP178
A	HIS293
A	TYR297
A	ILE304
A	TYR457
A	GLY458
A	VAL460

---

site_id	AC4
Number of Residues	29
Details	binding site for residue NAI A 604

Chain	Residue
A	ILE166
A	ILE167
A	PRO168
A	TRP169
A	ASN170
A	LYS193
A	ALA195
A	GLU196
A	GLY226
A	PRO227
A	GLY230
A	ALA231
A	PHE244
A	THR245
A	GLY246
A	SER247
A	VAL250
A	GLU269
A	LEU270
A	CYS303
A	GLN350
A	LYS353
A	GLU400
A	PHE402
A	YB602
A	CL605
A	CL610
A	HOH701
A	HOH749

---

site_id	AC5
Number of Residues	5
Details	binding site for residue CL A 605

Chain	Residue
A	GLU349
A	YB602
A	NAI604
A	CL610
A	CL611

---

site_id	AC6
Number of Residues	1
Details	binding site for residue CL A 606

Chain	Residue
A	ASP283

---

site_id	AC7
Number of Residues	1
Details	binding site for residue CL A 607

Chain	Residue
A	HOH747

---

site_id	AC8
Number of Residues	2
Details	binding site for residue CL A 609

Chain	Residue
A	THR155
A	HIS157

---

site_id	AC9
Number of Residues	6
Details	binding site for residue CL A 610

Chain	Residue
A	GLU349
A	YB602
A	NAI604
A	CL605
A	CL611
A	HOH859

---

site_id	AD1
Number of Residues	6
Details	binding site for residue CL A 611

Chain	Residue
A	GLU349
A	YB602
A	CL605
A	CL610
A	HOH842
A	HOH859

---

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

---

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

Chain	Residue	Details
A	LEU268-PRO275

---

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

---

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

---

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	LYS193
A	GLY226
A	GLY246
A	GLU269
A	GLU349
A	GLU400
A	ILE167

---

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

Chain	Residue	Details
A	ASN170

---

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

---

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

---

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

Chain	Residue	Details
A	THR337

---

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

Chain	Residue	Details
A	SER413

---