Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3QQP

Crystal Structure of 11beta-Hydroxysteroid Dehydrogenase 1 (11b-HSD1) in Complex with Urea Inhibitor

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	0016020	cellular_component	membrane
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	0016020	cellular_component	membrane
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	0016020	cellular_component	membrane
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	0016020	cellular_component	membrane
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	7
Details	BINDING SITE FOR RESIDUE S05 A 1

Chain	Residue
A	ILE121
A	SER170
A	TYR183
A	GLY216
A	LEU217
A	THR222
A	NDP293

site_id	AC2
Number of Residues	32
Details	BINDING SITE FOR RESIDUE NDP A 293

Chain	Residue
A	ALA42
A	SER43
A	LYS44
A	GLY45
A	ILE46
A	ALA65
A	ARG66
A	SER67
A	THR92
A	MET93
A	ASN119
A	ILE121
A	VAL168
A	SER169
A	SER170
A	TYR183
A	LYS187
A	LEU215
A	GLY216
A	LEU217
A	ILE218
A	THR220
A	THR222
A	ALA223
A	HOH310
A	HOH317
A	HOH319
A	HOH321
A	HOH328
A	HOH346
A	S051
A	GLY41

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE S05 B 2

Chain	Residue
B	SER170
B	TYR183
B	GLY216
B	LEU217
B	NDP293

site_id	AC4
Number of Residues	28
Details	BINDING SITE FOR RESIDUE NDP B 293

Chain	Residue
B	S052
B	GLY41
B	SER43
B	LYS44
B	GLY45
B	ILE46
B	ALA65
B	ARG66
B	SER67
B	THR92
B	MET93
B	ASN119
B	ILE121
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	HOH295
B	HOH296
B	HOH319

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE S05 C 3

Chain	Residue
C	SER170
C	VAL180
C	TYR183
C	GLY216
C	LEU217
C	THR222
C	NDP293

site_id	AC6
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NDP C 293

Chain	Residue
C	LEU215
C	GLY216
C	LEU217
C	ILE218
C	THR220
C	THR222
C	ALA223
C	HOH312
C	HOH322
C	HOH346
C	HOH347
C	S053
C	GLY41
C	SER43
C	LYS44
C	GLY45
C	ILE46
C	ALA65
C	ARG66
C	SER67
C	THR92
C	MET93
C	ASN119
C	HIS120
C	ILE121
C	ASN123
C	VAL168
C	SER169
C	SER170
C	TYR183
C	LYS187

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE S05 D 4

Chain	Residue
D	ILE121
D	SER170
D	TYR183
D	GLY216
D	LEU217
D	THR222
D	NDP293

site_id	AC8
Number of Residues	29
Details	BINDING SITE FOR RESIDUE NDP D 293

Chain	Residue
D	S054
D	GLY41
D	ALA42
D	SER43
D	LYS44
D	GLY45
D	ILE46
D	ALA65
D	ARG66
D	SER67
D	GLY91
D	THR92
D	MET93
D	ASN119
D	ILE121
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	HOH306
D	HOH322

Functional Information from PROSITE/UniProt

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

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"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	148
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15513927","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17919905","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18069989","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18485702","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18553955","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19217779","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15513927","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XU7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XU9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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