Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5PGY

CRYSTAL STRUCTURE OF 11BETA-HSD1 DOUBLE MUTANT (L262R, F278E) COMPLEXED WITH 2-[(5R,7S)-6-HYDROXY-2-PHENYLADAMANTAN-2-YL]-1-(3-HYDROXYAZETIDIN-1-YL)ETHAN-1-ONE (BMS-816336)

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
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
E	0005496	molecular_function	steroid binding
E	0005783	cellular_component	endoplasmic reticulum
E	0005789	cellular_component	endoplasmic reticulum membrane
E	0006629	biological_process	lipid metabolic process
E	0006706	biological_process	steroid catabolic process
E	0006713	biological_process	glucocorticoid catabolic process
E	0008202	biological_process	steroid metabolic process
E	0016020	cellular_component	membrane
E	0016491	molecular_function	oxidoreductase activity
E	0042803	molecular_function	protein homodimerization activity
E	0047022	molecular_function	7-beta-hydroxysteroid dehydrogenase (NADP+) activity
E	0050661	molecular_function	NADP binding
E	0070524	molecular_function	11-beta-hydroxysteroid dehydrogenase (NADP+) activity
E	0102196	molecular_function	cortisol dehydrogenase (NADP+) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	33
Details	binding site for residue NAP A 301

Chain	Residue
A	GLY41
A	THR92
A	MET93
A	ASN119
A	HIS120
A	ILE121
A	VAL168
A	SER169
A	TYR183
A	LYS187
A	LEU215
A	ALA42
A	GLY216
A	LEU217
A	ILE218
A	THR220
A	THR222
A	ALA223
A	8KG302
A	HOH403
A	HOH411
A	HOH413
A	SER43
A	HOH420
A	HOH429
A	HOH433
A	HOH440
A	LYS44
A	GLY45
A	ILE46
A	ALA65
A	ARG66
A	SER67

site_id	AC2
Number of Residues	11
Details	binding site for residue 8KG A 302

Chain	Residue
A	THR124
A	SER170
A	LEU171
A	TYR177
A	TYR183
A	GLY216
A	LEU217
A	THR222
A	ALA223
A	NAP301
A	HOH426

site_id	AC3
Number of Residues	30
Details	binding site for residue NAP B 301

Chain	Residue
B	GLY41
B	ALA42
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	TYR183
B	LYS187
B	LEU215
B	GLY216
B	LEU217
B	ILE218
B	THR220
B	THR222
B	ALA223
B	8KG302
B	HOH406
B	HOH426
B	HOH427
B	HOH431
B	HOH441

site_id	AC4
Number of Residues	13
Details	binding site for residue 8KG B 302

Chain	Residue
B	THR124
B	SER170
B	LEU171
B	TYR177
B	TYR183
B	GLY216
B	LEU217
B	ALA223
B	VAL227
B	NAP301
B	HOH405
B	HOH414
B	HOH418

site_id	AC5
Number of Residues	33
Details	binding site for residue NAP D 301

Chain	Residue
D	ILE121
D	VAL168
D	SER169
D	TYR183
D	LYS187
D	LEU215
D	GLY216
D	LEU217
D	ILE218
D	THR220
D	THR222
D	ALA223
D	8KG302
D	HOH402
D	HOH408
D	HOH410
D	HOH417
D	HOH427
D	HOH428
D	HOH451
D	HOH454
D	GLY41
D	ALA42
D	SER43
D	LYS44
D	GLY45
D	ILE46
D	ALA65
D	ARG66
D	SER67
D	THR92
D	MET93
D	ASN119

site_id	AC6
Number of Residues	11
Details	binding site for residue 8KG D 302

Chain	Residue
D	THR124
D	SER170
D	LEU171
D	TYR177
D	TYR183
D	GLY216
D	LEU217
D	THR222
D	NAP301
D	HOH441
E	TYR284

site_id	AC7
Number of Residues	28
Details	binding site for residue NAP E 301

Chain	Residue
E	GLY41
E	SER43
E	LYS44
E	GLY45
E	ILE46
E	ARG66
E	SER67
E	THR92
E	MET93
E	ASN119
E	ILE121
E	VAL168
E	SER169
E	TYR183
E	LYS187
E	LEU215
E	GLY216
E	LEU217
E	ILE218
E	THR220
E	THR222
E	ALA223
E	8KG302
E	HOH432
E	HOH437
E	HOH440
E	HOH442
E	HOH443

site_id	AC8
Number of Residues	12
Details	binding site for residue 8KG E 302

Chain	Residue
E	THR124
E	SER170
E	LEU171
E	TYR177
E	TYR183
E	GLY216
E	LEU217
E	THR222
E	ALA223
E	MET233
E	NAP301
E	HOH444

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)