Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1XU7

Crystal Structure of the Interface Open Conformation of Tetrameric 11b-HSD1

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	36
Details	BINDING SITE FOR RESIDUE NDP A 522

Chain	Residue
A	GLY41
A	MET93
A	ASN119
A	HIS120
A	ILE121
A	VAL168
A	SER169
A	SER170
A	TYR183
A	LYS187
A	LEU215
A	SER43
A	GLY216
A	LEU217
A	ILE218
A	THR220
A	THR222
A	ALA223
A	CPS523
A	HOH536
A	HOH543
A	HOH557
A	LYS44
A	HOH597
A	HOH618
A	HOH685
A	HOH744
A	HOH797
A	HOH803
A	HOH964
A	GLY45
A	ILE46
A	ALA65
A	ARG66
A	SER67
A	THR92

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CPS A 523

Chain	Residue
A	ILE121
A	LEU171
A	TYR177
A	TYR183
A	LEU217
A	ALA223
A	VAL227
A	GLN234
A	SER260
A	SER261
A	THR264
A	NDP522
A	HOH546
A	HOH580
B	TYR280
B	HOH921

site_id	AC3
Number of Residues	36
Details	BINDING SITE FOR RESIDUE NDP B 524

Chain	Residue
B	GLY41
B	SER43
B	LYS44
B	GLY45
B	ILE46
B	ALA65
B	ARG66
B	SER67
B	THR92
B	MET93
B	ASN119
B	HIS120
B	ILE121
B	VAL168
B	SER169
B	SER170
B	TYR183
B	LYS187
B	LEU215
B	GLY216
B	ILE218
B	THR220
B	THR222
B	ALA223
B	CPS525
B	HOH567
B	HOH575
B	HOH617
B	HOH642
B	HOH686
B	HOH741
B	HOH795
B	HOH820
B	HOH830
B	HOH945
B	HOH1000

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CPS B 525

Chain	Residue
B	NDP524
B	HOH550
B	HOH823
A	TYR280
A	HOH861
B	ILE121
B	LEU171
B	TYR177
B	TYR183
B	LEU217
B	ALA223
B	MET233
B	GLN234
B	THR264

site_id	AC5
Number of Residues	34
Details	BINDING SITE FOR RESIDUE NDP C 526

Chain	Residue
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	VAL168
C	SER169
C	SER170
C	TYR183
C	LYS187
C	LEU215
C	GLY216
C	LEU217
C	ILE218
C	THR220
C	THR222
C	ALA223
C	CPS527
C	HOH566
C	HOH569
C	HOH625
C	HOH707
C	HOH793
C	HOH834
C	HOH932
C	HOH954

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CPS C 527

Chain	Residue
C	ILE121
C	THR124
C	LEU171
C	TYR177
C	TYR183
C	LEU217
C	ALA223
C	MET233
C	GLN234
C	THR264
C	NDP526
C	HOH801
C	HOH872
D	TYR280
D	HOH897

site_id	AC7
Number of Residues	33
Details	BINDING SITE FOR RESIDUE NDP D 528

Chain	Residue
D	GLY41
D	SER43
D	LYS44
D	GLY45
D	ILE46
D	ALA65
D	ARG66
D	SER67
D	THR92
D	MET93
D	ASN119
D	HIS120
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	CPS529
D	HOH560
D	HOH576
D	HOH603
D	HOH606
D	HOH635
D	HOH829
D	HOH965

site_id	AC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CPS D 529

Chain	Residue
C	TYR280
C	HOH708
D	ILE121
D	LEU171
D	TYR177
D	TYR183
D	LEU217
D	ALA223
D	MET233
D	GLN234
D	NDP528
D	HOH584
D	HOH796
D	HOH884

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CPS A 1

Chain	Residue
A	PRO271
A	SER272
A	ILE275
A	HOH998
C	LEU266
C	PRO271
D	SER272

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CPS C 2

Chain	Residue
A	LEU266
B	SER272
C	PRO271
C	SER272
C	ILE275

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

Catalytic Information from CSA

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

Chain	Residue	Details
A	LYS174

site_id	CSA10
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	CSA11
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	CSA12
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	CSA13
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	LYS187
A	VAL180

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

Chain	Residue	Details
B	LYS187
B	VAL180

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

Chain	Residue	Details
C	LYS187
C	VAL180

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

Chain	Residue	Details
D	LYS187
D	VAL180

site_id	CSA17
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	LYS187
A	TYR183

site_id	CSA18
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
B	LYS187
B	TYR183

site_id	CSA19
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
C	LYS187
C	TYR183

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

Chain	Residue	Details
B	LYS174

site_id	CSA20
Number of Residues	2
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
D	LYS187
D	TYR183

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

Chain	Residue	Details
C	LYS174

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

Chain	Residue	Details
D	LYS174

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	LYS187
A	SER170
A	TYR183

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
B	LYS187
B	SER170
B	TYR183

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
C	LYS187
C	SER170
C	TYR183

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
D	LYS187
D	SER170
D	TYR183

site_id	CSA9
Number of Residues	4
Details	Annotated By Reference To The Literature 1eq2

Chain	Residue	Details
A	LYS187
A	SER170
A	TYR183
A	ASN143

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)