Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3CV6

The crystal structure of mouse 17-alpha hydroxysteroid dehydrogenase GG225.226PP mutant in complex with inhibitor and cofactor NADP+.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004032	molecular_function	aldose reductase (NADPH) activity
A	0004033	molecular_function	aldo-keto reductase (NADPH) activity
A	0005496	molecular_function	steroid binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006629	biological_process	lipid metabolic process
A	0006693	biological_process	prostaglandin metabolic process
A	0006694	biological_process	steroid biosynthetic process
A	0008202	biological_process	steroid metabolic process
A	0016229	molecular_function	steroid dehydrogenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0032052	molecular_function	bile acid binding
A	0033764	molecular_function	steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0042448	biological_process	progesterone metabolic process
A	0044597	biological_process	daunorubicin metabolic process
A	0044598	biological_process	doxorubicin metabolic process
A	0047023	molecular_function	androsterone dehydrogenase activity
A	0047024	molecular_function	5alpha-androstane-3beta,17beta-diol dehydrogenase activity
A	0047086	molecular_function	ketosteroid monooxygenase activity
A	0070401	molecular_function	NADP+ binding
A	0070402	molecular_function	NADPH binding
A	0072555	molecular_function	17-beta-ketosteroid reductase activity
A	0072582	molecular_function	17-beta-hydroxysteroid dehydrogenase (NADP+) activity
A	1902121	molecular_function	lithocholic acid binding
B	0004032	molecular_function	aldose reductase (NADPH) activity
B	0004033	molecular_function	aldo-keto reductase (NADPH) activity
B	0005496	molecular_function	steroid binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006629	biological_process	lipid metabolic process
B	0006693	biological_process	prostaglandin metabolic process
B	0006694	biological_process	steroid biosynthetic process
B	0008202	biological_process	steroid metabolic process
B	0016229	molecular_function	steroid dehydrogenase activity
B	0016491	molecular_function	oxidoreductase activity
B	0032052	molecular_function	bile acid binding
B	0033764	molecular_function	steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0042448	biological_process	progesterone metabolic process
B	0044597	biological_process	daunorubicin metabolic process
B	0044598	biological_process	doxorubicin metabolic process
B	0047023	molecular_function	androsterone dehydrogenase activity
B	0047024	molecular_function	5alpha-androstane-3beta,17beta-diol dehydrogenase activity
B	0047086	molecular_function	ketosteroid monooxygenase activity
B	0070401	molecular_function	NADP+ binding
B	0070402	molecular_function	NADPH binding
B	0072555	molecular_function	17-beta-ketosteroid reductase activity
B	0072582	molecular_function	17-beta-hydroxysteroid dehydrogenase (NADP+) activity
B	1902121	molecular_function	lithocholic acid binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAP A 350

Chain	Residue
A	GLY22
A	TYR216
A	GLY217
A	LEU219
A	GLY220
A	THR221
A	GLN222
A	TYR224
A	LEU236
A	ALA253
A	ASN269
A	THR23
A	THR270
A	SER271
A	LEU272
A	LYS273
A	ARG276
A	GLU279
A	ASN280
A	ALA24
A	ASP50
A	TYR55
A	HIS117
A	SER166
A	ASN167
A	GLN190

site_id	AC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAP B 350

Chain	Residue
B	GLY22
B	THR23
B	ALA24
B	ASP50
B	TYR55
B	HIS117
B	SER166
B	ASN167
B	GLN190
B	TYR216
B	GLY217
B	LEU219
B	GLY220
B	THR221
B	GLN222
B	TYR224
B	ALA253
B	ASN269
B	THR270
B	SER271
B	LEU272
B	LYS273
B	ARG276
B	GLU279
B	ASN280

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE HXS A 351

Chain	Residue
A	ALA24
A	LEU25
A	LEU27
A	LYS31
A	TYR55
A	HIS117
A	TYR118
A	TYR224
A	TRP227

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE HXS B 351

Chain	Residue
B	ALA24
B	LEU25
B	LYS31
B	TYR55
B	HIS117
B	TYR118
B	TYR224
B	TRP227

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE BME A 352

Chain	Residue
A	CYS29

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE BME A 353

Chain	Residue
A	HIS6

Functional Information from PROSITE/UniProt

site_id	PS00062
Number of Residues	18
Details	ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MekckdaglTKSIGVSNF

Chain	Residue	Details
A	MET151-PHE168

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor

Chain	Residue	Details
A	TYR55
B	TYR55

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:17034817, ECO:0000269\|PubMed:17909281, ECO:0000269\|PubMed:19237748

Chain	Residue	Details
A	GLY20
B	GLN190
B	TYR216
B	THR270
A	ASP50
A	SER166
A	GLN190
A	TYR216
A	THR270
B	GLY20
B	ASP50
B	SER166

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	LYS31
A	HIS117
B	LYS31
B	HIS117

site_id	SWS_FT_FI4
Number of Residues	2
Details	SITE: Lowers pKa of active site Tyr => ECO:0000250

Chain	Residue	Details
A	LYS84
B	LYS84

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)