Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3TFQ

Crystal structure of 11b-hsd1 double mutant (l262r, f278e) complexed with 8-{[(2-CYANOPYRIDIN-3-YL)METHYL]SULFANYL}-6-HYDROXY-3,4-DIHYDRO-1H-PYRANO[3,4-C]PYRIDINE-5-CARBONITRILE

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	0006706	biological_process	steroid catabolic process
A	0008202	biological_process	steroid metabolic process
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0030324	biological_process	lung development
A	0042803	molecular_function	protein homodimerization activity
A	0043231	cellular_component	intracellular membrane-bounded organelle
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 activity
B	0005496	molecular_function	steroid binding
B	0005783	cellular_component	endoplasmic reticulum
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0006706	biological_process	steroid catabolic process
B	0008202	biological_process	steroid metabolic process
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0030324	biological_process	lung development
B	0042803	molecular_function	protein homodimerization activity
B	0043231	cellular_component	intracellular membrane-bounded organelle
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 activity
D	0005496	molecular_function	steroid binding
D	0005783	cellular_component	endoplasmic reticulum
D	0005789	cellular_component	endoplasmic reticulum membrane
D	0006706	biological_process	steroid catabolic process
D	0008202	biological_process	steroid metabolic process
D	0016020	cellular_component	membrane
D	0016491	molecular_function	oxidoreductase activity
D	0030324	biological_process	lung development
D	0042803	molecular_function	protein homodimerization activity
D	0043231	cellular_component	intracellular membrane-bounded organelle
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 activity
E	0005496	molecular_function	steroid binding
E	0005783	cellular_component	endoplasmic reticulum
E	0005789	cellular_component	endoplasmic reticulum membrane
E	0006706	biological_process	steroid catabolic process
E	0008202	biological_process	steroid metabolic process
E	0016020	cellular_component	membrane
E	0016491	molecular_function	oxidoreductase activity
E	0030324	biological_process	lung development
E	0042803	molecular_function	protein homodimerization activity
E	0043231	cellular_component	intracellular membrane-bounded organelle
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 activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	34
Details	BINDING SITE FOR RESIDUE NAP A 301

Chain	Residue
A	GLY41
A	THR92
A	MET93
A	ASN119
A	ILE121
A	VAL168
A	SER169
A	TYR183
A	LYS187
A	LEU215
A	GLY216
A	ALA42
A	LEU217
A	ILE218
A	THR220
A	THR222
A	ALA223
A	07M302
A	HOH406
A	HOH409
A	HOH413
A	HOH425
A	SER43
A	HOH428
A	HOH437
A	HOH452
A	HOH465
A	HOH580
A	LYS44
A	GLY45
A	ILE46
A	ALA65
A	ARG66
A	SER67

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 07M A 302

Chain	Residue
A	THR124
A	SER125
A	LEU126
A	SER170
A	LEU171
A	TYR183
A	LEU215
A	GLY216
A	THR222
A	ALA226
A	NAP301

site_id	AC3
Number of Residues	33
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	07M302
B	HOH402
B	HOH408
B	HOH412
B	HOH424
B	HOH425
B	HOH428
B	HOH474
B	HOH485

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 07M B 302

Chain	Residue
A	HOH598
B	THR124
B	SER125
B	SER170
B	LEU171
B	TYR183
B	LEU215
B	GLY216
B	THR222
B	ALA226
B	NAP301

site_id	AC5
Number of Residues	35
Details	BINDING SITE FOR RESIDUE NAP D 301

Chain	Residue
D	MET93
D	ASN119
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	07M302
D	HOH401
D	HOH403
D	HOH416
D	HOH421
D	HOH427
D	HOH436
D	HOH466
D	HOH517
D	HOH524
D	HOH607
D	GLY41
D	ALA42
D	SER43
D	LYS44
D	GLY45
D	ILE46
D	ALA65
D	ARG66
D	SER67
D	THR92

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 07M D 302

Chain	Residue
D	ILE121
D	THR124
D	SER125
D	LEU126
D	SER170
D	LEU171
D	TYR183
D	LEU215
D	GLY216
D	THR222
D	ALA226
D	NAP301
D	HOH512

site_id	AC7
Number of Residues	33
Details	BINDING SITE FOR RESIDUE NAP E 301

Chain	Residue
E	GLY41
E	ALA42
E	SER43
E	LYS44
E	GLY45
E	ILE46
E	ALA65
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	07M302
E	HOH403
E	HOH420
E	HOH431
E	HOH433
E	HOH447
E	HOH448
E	HOH477
E	HOH520

site_id	AC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 07M E 302

Chain	Residue
D	HOH611
E	ILE121
E	THR124
E	SER125
E	SER170
E	LEU171
E	TYR183
E	LEU215
E	GLY216
E	THR222
E	ALA226
E	MET233
E	NAP301

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL E 351

Chain	Residue
E	ASN207
E	SER209
E	ARG252
E	HOH418

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	1068
Details	TOPO_DOM: Lumenal => ECO:0000255

Chain	Residue	Details
A	GLU25-LYS292
B	GLU25-LYS292
D	GLU25-LYS292
E	GLU25-LYS292

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	TYR183
B	TYR183
D	TYR183
E	TYR183

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269\|PubMed:15513927, ECO:0000269\|PubMed:17919905, ECO:0000269\|PubMed:18069989, ECO:0000269\|PubMed:18485702, ECO:0000269\|PubMed:18553955, ECO:0000269\|PubMed:19217779

Chain	Residue	Details
A	GLY41
B	ILE218
D	GLY41
D	THR92
D	ASN119
D	TYR183
D	ILE218
E	GLY41
E	THR92
E	ASN119
E	TYR183
A	THR92
E	ILE218
A	ASN119
A	TYR183
A	ILE218
B	GLY41
B	THR92
B	ASN119
B	TYR183

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:15513927, ECO:0007744\|PDB:1XU7, ECO:0007744\|PDB:1XU9

Chain	Residue	Details
A	SER170
B	SER170
D	SER170
E	SER170

site_id	SWS_FT_FI5
Number of Residues	8
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:19159218

Chain	Residue	Details
A	ASN123
A	ASN162
B	ASN123
B	ASN162
D	ASN123
D	ASN162
E	ASN123
E	ASN162

site_id	SWS_FT_FI6
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN207
B	ASN207
D	ASN207
E	ASN207

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