Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3DWF

Crystal Structure of the Guinea Pig 11beta-Hydroxysteroid Dehydrogenase Type 1 Mutant F278E

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005496	molecular_function	steroid binding
A	0005783	cellular_component	endoplasmic reticulum
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0006629	biological_process	lipid metabolic process
A	0006706	biological_process	steroid catabolic process
A	0006713	biological_process	glucocorticoid catabolic process
A	0008202	biological_process	steroid metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0042803	molecular_function	protein homodimerization activity
A	0047022	molecular_function	7-beta-hydroxysteroid dehydrogenase (NADP+) activity
A	0050661	molecular_function	NADP binding
A	0070524	molecular_function	11-beta-hydroxysteroid dehydrogenase (NADP+) activity
A	0102196	molecular_function	cortisol dehydrogenase (NADP+) activity
B	0005496	molecular_function	steroid binding
B	0005783	cellular_component	endoplasmic reticulum
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0006629	biological_process	lipid metabolic process
B	0006706	biological_process	steroid catabolic process
B	0006713	biological_process	glucocorticoid catabolic process
B	0008202	biological_process	steroid metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0042803	molecular_function	protein homodimerization activity
B	0047022	molecular_function	7-beta-hydroxysteroid dehydrogenase (NADP+) activity
B	0050661	molecular_function	NADP binding
B	0070524	molecular_function	11-beta-hydroxysteroid dehydrogenase (NADP+) activity
B	0102196	molecular_function	cortisol dehydrogenase (NADP+) activity
C	0005496	molecular_function	steroid binding
C	0005783	cellular_component	endoplasmic reticulum
C	0005789	cellular_component	endoplasmic reticulum membrane
C	0006629	biological_process	lipid metabolic process
C	0006706	biological_process	steroid catabolic process
C	0006713	biological_process	glucocorticoid catabolic process
C	0008202	biological_process	steroid metabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0042803	molecular_function	protein homodimerization activity
C	0047022	molecular_function	7-beta-hydroxysteroid dehydrogenase (NADP+) activity
C	0050661	molecular_function	NADP binding
C	0070524	molecular_function	11-beta-hydroxysteroid dehydrogenase (NADP+) activity
C	0102196	molecular_function	cortisol dehydrogenase (NADP+) activity
D	0005496	molecular_function	steroid binding
D	0005783	cellular_component	endoplasmic reticulum
D	0005789	cellular_component	endoplasmic reticulum membrane
D	0006629	biological_process	lipid metabolic process
D	0006706	biological_process	steroid catabolic process
D	0006713	biological_process	glucocorticoid catabolic process
D	0008202	biological_process	steroid metabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0042803	molecular_function	protein homodimerization activity
D	0047022	molecular_function	7-beta-hydroxysteroid dehydrogenase (NADP+) activity
D	0050661	molecular_function	NADP binding
D	0070524	molecular_function	11-beta-hydroxysteroid dehydrogenase (NADP+) activity
D	0102196	molecular_function	cortisol dehydrogenase (NADP+) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAP A 301

Chain	Residue
A	HOH4
A	SER67
A	GLY91
A	SER92
A	MET93
A	ASN119
A	HIS120
A	VAL121
A	TYR123
A	VAL168
A	SER169
A	GOL9
A	SER170
A	TYR183
A	LYS187
A	LEU215
A	GLY216
A	LEU217
A	ILE218
A	THR220
A	THR222
A	ALA223
A	GLY41
A	HOH315
A	HOH332
A	SER43
A	LYS44
A	GLY45
A	ILE46
A	ALA65
A	ARG66

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 A 1

Chain	Residue
A	LYS44
A	GLY45
A	ARG48
A	THR220
A	GLU221
A	LYS238
A	HOH300
A	HOH332
A	HOH671
D	LYS138

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL A 9

Chain	Residue
A	NAP301

site_id	AC4
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAP B 301

Chain	Residue
B	HOH23
B	GLY41
B	SER43
B	LYS44
B	GLY45
B	ILE46
B	ALA65
B	ARG66
B	SER67
B	GLY91
B	SER92
B	MET93
B	ASN119
B	HIS120
B	VAL121
B	VAL168
B	SER169
B	SER170
B	TYR183
B	LYS187
B	LEU215
B	GLY216
B	LEU217
B	ILE218
B	THR220
B	THR222
B	ALA223
B	HOH300
B	HOH305
B	HOH323
B	HOH346

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 B 2

Chain	Residue
B	LYS44
B	GLY45
B	ARG48
B	THR220
B	GLU221
B	LYS238
B	HOH323
B	HOH338

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 4

Chain	Residue
B	ARG48
B	LYS73
B	HOH413

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL B 6

Chain	Residue
B	SER170

site_id	AC8
Number of Residues	29
Details	BINDING SITE FOR RESIDUE NAP C 301

Chain	Residue
C	TYR123
C	VAL168
C	SER169
C	SER170
C	TYR183
C	LYS187
C	LEU215
C	GLY216
C	LEU217
C	ILE218
C	THR220
C	THR222
C	ALA223
C	HOH303
C	HOH308
C	GLY41
C	SER43
C	LYS44
C	GLY45
C	ILE46
C	ALA65
C	ARG66
C	SER67
C	GLY91
C	SER92
C	MET93
C	ASN119
C	HIS120
C	VAL121

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 3

Chain	Residue
B	HOH351
C	GLY45
C	ARG48
C	THR220
C	GLU221
C	LYS238
C	HOH1126

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 5

Chain	Residue
B	ARG66
B	SER92
C	ARG48
C	HOH1186

site_id	BC2
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAP D 301

Chain	Residue
D	HOH9
D	GLY41
D	SER43
D	LYS44
D	GLY45
D	ILE46
D	ALA65
D	ARG66
D	SER67
D	GLY91
D	SER92
D	MET93
D	ASN119
D	HIS120
D	VAL121
D	VAL168
D	SER169
D	SER170
D	TYR183
D	LYS187
D	LEU215
D	GLY216
D	LEU217
D	ILE218
D	THR220
D	THR222
D	ALA223
D	HOH303
D	HOH306
D	HOH378

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 4

Chain	Residue
D	GLY45
D	ARG48
D	THR220
D	GLU221
D	LYS238
D	HOH306

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL D 1

Chain	Residue
C	LYS174
C	PHE188
C	ASP191
C	ARG273
D	LYS174
D	PHE188
D	ARG273
D	HOH321
D	HOH400

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 2

Chain	Residue
A	SER261
A	HOH326
D	SER261
D	ARG262
D	TRP263

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 5

Chain	Residue
D	ASN204
D	VAL206
D	TYR296
D	GLY297
D	TRP299

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL D 7

Chain	Residue
D	ARG48
D	LYS73

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL D 8

Chain	Residue
A	ARG48
D	ARG66
D	SER92
D	GLU94

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER170-ARG198

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10001","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	156
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15542590","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19473839","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19507261","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	LYS187
A	SER170
A	TYR183

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
B	LYS187
B	ILE180

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
C	LYS187
C	ILE180

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
D	LYS187
D	ILE180

site_id	CSA13
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	LYS187
A	TYR183

site_id	CSA14
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
B	LYS187
B	TYR183

site_id	CSA15
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
C	LYS187
C	TYR183

site_id	CSA16
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
D	LYS187
D	TYR183

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
B	LYS187
B	SER170
B	TYR183

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
C	LYS187
C	SER170
C	TYR183

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
D	LYS187
D	SER170
D	TYR183

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	LYS187
A	SER170
A	TYR183
A	ASN143

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
B	LYS187
B	SER170
B	TYR183
B	ASN143

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
C	LYS187
C	SER170
C	TYR183
C	ASN143

site_id	CSA8
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
D	LYS187
D	SER170
D	TYR183
D	ASN143

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	LYS187
A	ILE180

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