Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7ENY

Crystal structure of hydroxysteroid dehydrogenase from Escherichia coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005829	cellular_component	cytosol
A	0008709	molecular_function	cholate 7-alpha-dehydrogenase activity
A	0016042	biological_process	lipid catabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0030573	biological_process	bile acid catabolic process
A	0032991	cellular_component	protein-containing complex
A	0042802	molecular_function	identical protein binding
A	0051287	molecular_function	NAD binding
A	0106281	molecular_function	chenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity
B	0005829	cellular_component	cytosol
B	0008709	molecular_function	cholate 7-alpha-dehydrogenase activity
B	0016042	biological_process	lipid catabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0030573	biological_process	bile acid catabolic process
B	0032991	cellular_component	protein-containing complex
B	0042802	molecular_function	identical protein binding
B	0051287	molecular_function	NAD binding
B	0106281	molecular_function	chenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity
C	0005829	cellular_component	cytosol
C	0008709	molecular_function	cholate 7-alpha-dehydrogenase activity
C	0016042	biological_process	lipid catabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0030573	biological_process	bile acid catabolic process
C	0032991	cellular_component	protein-containing complex
C	0042802	molecular_function	identical protein binding
C	0051287	molecular_function	NAD binding
C	0106281	molecular_function	chenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity
D	0005829	cellular_component	cytosol
D	0008709	molecular_function	cholate 7-alpha-dehydrogenase activity
D	0016042	biological_process	lipid catabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0030573	biological_process	bile acid catabolic process
D	0032991	cellular_component	protein-containing complex
D	0042802	molecular_function	identical protein binding
D	0051287	molecular_function	NAD binding
D	0106281	molecular_function	chenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity
E	0005829	cellular_component	cytosol
E	0008709	molecular_function	cholate 7-alpha-dehydrogenase activity
E	0016042	biological_process	lipid catabolic process
E	0016491	molecular_function	oxidoreductase activity
E	0030573	biological_process	bile acid catabolic process
E	0032991	cellular_component	protein-containing complex
E	0042802	molecular_function	identical protein binding
E	0051287	molecular_function	NAD binding
E	0106281	molecular_function	chenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity
F	0005829	cellular_component	cytosol
F	0008709	molecular_function	cholate 7-alpha-dehydrogenase activity
F	0016042	biological_process	lipid catabolic process
F	0016491	molecular_function	oxidoreductase activity
F	0030573	biological_process	bile acid catabolic process
F	0032991	cellular_component	protein-containing complex
F	0042802	molecular_function	identical protein binding
F	0051287	molecular_function	NAD binding
F	0106281	molecular_function	chenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity
G	0005829	cellular_component	cytosol
G	0008709	molecular_function	cholate 7-alpha-dehydrogenase activity
G	0016042	biological_process	lipid catabolic process
G	0016491	molecular_function	oxidoreductase activity
G	0030573	biological_process	bile acid catabolic process
G	0032991	cellular_component	protein-containing complex
G	0042802	molecular_function	identical protein binding
G	0051287	molecular_function	NAD binding
G	0106281	molecular_function	chenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity
H	0005829	cellular_component	cytosol
H	0008709	molecular_function	cholate 7-alpha-dehydrogenase activity
H	0016042	biological_process	lipid catabolic process
H	0016491	molecular_function	oxidoreductase activity
H	0030573	biological_process	bile acid catabolic process
H	0032991	cellular_component	protein-containing complex
H	0042802	molecular_function	identical protein binding
H	0051287	molecular_function	NAD binding
H	0106281	molecular_function	chenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity

Functional Information from PROSITE/UniProt

site_id	PS00061
Number of Residues	29
Details	ADH_SHORT Short-chain dehydrogenases/reductases family signature. SmaaenkninMtsYASSKAAAsHLVrNMA

Chain	Residue	Details
A	SER146-ALA174

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton acceptor => ECO:0000305\|PubMed:8672472, ECO:0000305\|PubMed:9722677

Chain	Residue	Details
A	TYR159
B	TYR159
C	TYR159
D	TYR159
E	TYR159
F	TYR159
G	TYR159
H	TYR159

site_id	SWS_FT_FI2
Number of Residues	40
Details	BINDING: BINDING => ECO:0000269\|PubMed:8672472, ECO:0007744\|PDB:1AHI, ECO:0007744\|PDB:1FMC

Chain	Residue	Details
A	ILE23
B	TYR159
C	ILE23
C	GLY99
C	SER146
C	ASN151
C	TYR159
D	ILE23
D	GLY99
D	SER146
D	ASN151
A	GLY99
D	TYR159
E	ILE23
E	GLY99
E	SER146
E	ASN151
E	TYR159
F	ILE23
F	GLY99
F	SER146
F	ASN151
A	SER146
F	TYR159
G	ILE23
G	GLY99
G	SER146
G	ASN151
G	TYR159
H	ILE23
H	GLY99
H	SER146
H	ASN151
A	ASN151
H	TYR159
A	TYR159
B	ILE23
B	GLY99
B	SER146
B	ASN151

site_id	SWS_FT_FI3
Number of Residues	40
Details	BINDING: BINDING => ECO:0000269\|PubMed:8672472, ECO:0007744\|PDB:1AHH, ECO:0007744\|PDB:1AHI, ECO:0007744\|PDB:1FMC

Chain	Residue	Details
A	ASP42
B	ILE192
C	ASP42
C	ASP68
C	ASN95
C	LYS163
C	ILE192
D	ASP42
D	ASP68
D	ASN95
D	LYS163
A	ASP68
D	ILE192
E	ASP42
E	ASP68
E	ASN95
E	LYS163
E	ILE192
F	ASP42
F	ASP68
F	ASN95
F	LYS163
A	ASN95
F	ILE192
G	ASP42
G	ASP68
G	ASN95
G	LYS163
G	ILE192
H	ASP42
H	ASP68
H	ASN95
H	LYS163
A	LYS163
H	ILE192
A	ILE192
B	ASP42
B	ASP68
B	ASN95
B	LYS163

site_id	SWS_FT_FI4
Number of Residues	8
Details	SITE: Transition state stabilizer => ECO:0000305\|PubMed:8672472, ECO:0000305\|PubMed:9722677

Chain	Residue	Details
A	SER146
B	SER146
C	SER146
D	SER146
E	SER146
F	SER146
G	SER146
H	SER146

site_id	SWS_FT_FI5
Number of Residues	8
Details	SITE: Lowers pKa of active site Tyr => ECO:0000305\|PubMed:8672472, ECO:0000305\|PubMed:9722677

Chain	Residue	Details
A	LYS163
B	LYS163
C	LYS163
D	LYS163
E	LYS163
F	LYS163
G	LYS163
H	LYS163

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