Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3P2L

Crystal Structure of ATP-dependent Clp protease subunit P from Francisella tularensis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004176	molecular_function	ATP-dependent peptidase activity
A	0004252	molecular_function	serine-type endopeptidase activity
A	0005737	cellular_component	cytoplasm
A	0006508	biological_process	proteolysis
A	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
A	0008236	molecular_function	serine-type peptidase activity
A	0009368	cellular_component	endopeptidase Clp complex
A	0051117	molecular_function	ATPase binding
B	0004176	molecular_function	ATP-dependent peptidase activity
B	0004252	molecular_function	serine-type endopeptidase activity
B	0005737	cellular_component	cytoplasm
B	0006508	biological_process	proteolysis
B	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
B	0008236	molecular_function	serine-type peptidase activity
B	0009368	cellular_component	endopeptidase Clp complex
B	0051117	molecular_function	ATPase binding
C	0004176	molecular_function	ATP-dependent peptidase activity
C	0004252	molecular_function	serine-type endopeptidase activity
C	0005737	cellular_component	cytoplasm
C	0006508	biological_process	proteolysis
C	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
C	0008236	molecular_function	serine-type peptidase activity
C	0009368	cellular_component	endopeptidase Clp complex
C	0051117	molecular_function	ATPase binding
D	0004176	molecular_function	ATP-dependent peptidase activity
D	0004252	molecular_function	serine-type endopeptidase activity
D	0005737	cellular_component	cytoplasm
D	0006508	biological_process	proteolysis
D	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
D	0008236	molecular_function	serine-type peptidase activity
D	0009368	cellular_component	endopeptidase Clp complex
D	0051117	molecular_function	ATPase binding
E	0004176	molecular_function	ATP-dependent peptidase activity
E	0004252	molecular_function	serine-type endopeptidase activity
E	0005737	cellular_component	cytoplasm
E	0006508	biological_process	proteolysis
E	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
E	0008236	molecular_function	serine-type peptidase activity
E	0009368	cellular_component	endopeptidase Clp complex
E	0051117	molecular_function	ATPase binding
F	0004176	molecular_function	ATP-dependent peptidase activity
F	0004252	molecular_function	serine-type endopeptidase activity
F	0005737	cellular_component	cytoplasm
F	0006508	biological_process	proteolysis
F	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
F	0008236	molecular_function	serine-type peptidase activity
F	0009368	cellular_component	endopeptidase Clp complex
F	0051117	molecular_function	ATPase binding
G	0004176	molecular_function	ATP-dependent peptidase activity
G	0004252	molecular_function	serine-type endopeptidase activity
G	0005737	cellular_component	cytoplasm
G	0006508	biological_process	proteolysis
G	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
G	0008236	molecular_function	serine-type peptidase activity
G	0009368	cellular_component	endopeptidase Clp complex
G	0051117	molecular_function	ATPase binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 202

Chain	Residue
A	MSE84
A	ILE87
A	PRO89
A	PO4212
A	HOH259

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG A 203

Chain	Residue
A	TYR66
A	ARG196
A	HOH293

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 204

Chain	Residue
A	MSE102
A	SER104
A	ILE125
A	HIS126
A	HOH298
A	SER101

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG A 205

Chain	Residue
A	PRO70
A	SER101

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 206

Chain	Residue
A	ASN176
A	MSE178
A	GLU182
A	HOH330

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG A 207

Chain	Residue
A	TYR81
D	SER120

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 208

Chain	Residue
A	LYS184
A	HIS191
A	VAL192

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 209

Chain	Residue
A	THR161
A	GLN163
A	ALA185
A	GOL211

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 210

Chain	Residue
A	HOH225
A	HOH229
A	HOH309

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 211

Chain	Residue
A	LYS112
A	ARG115
A	HIS160
A	THR161
A	GOL209

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 A 212

Chain	Residue
A	GLN85
A	ILE87
A	LYS88
A	ASP90
A	MG202
A	HOH248

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 202

Chain	Residue
B	MSE84
B	ILE87
B	PRO89
B	PO4204
B	HOH220

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 B 203

Chain	Residue
B	LYS184
B	HIS191

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 B 204

Chain	Residue
B	GLN85
B	ILE87
B	LYS88
B	ASP90
B	MG202

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG B 205

Chain	Residue
B	TYR66
B	ARG196
B	HOH295
B	HOH296

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEG B 206

Chain	Residue
B	VAL74
B	SER101
B	HIS126
B	GLN127
B	PRO128
B	LEU129
B	PEG207

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PEG B 207

Chain	Residue
B	PRO70
B	GLY71
B	GLY72
B	SER101
B	LEU129
B	PEG206

site_id	BC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL B 208

Chain	Residue
B	GLU182

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 209

Chain	Residue
B	PHE34
B	ASN36
C	ASN45
G	LEU6

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG B 211

Chain	Residue
A	LYS61
B	THR161
B	GLY162
B	ALA185
B	GLY187

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 202

Chain	Residue
C	MSE84
C	ILE87
C	PRO89
C	PO4209
C	HOH232
C	HOH233

site_id	CC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG C 203

Chain	Residue
C	TYR66
C	ARG196

site_id	CC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEG C 204

Chain	Residue
C	SER101
C	SER104
C	ILE125
C	HIS126
C	GLN127
C	PRO128
C	HOH219

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 205

Chain	Residue
C	HOH297
C	PRO70
C	SER101

site_id	CC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG C 206

Chain	Residue
C	LYS184
C	HIS191
C	VAL192

site_id	CC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO C 207

Chain	Residue
C	LYS112
C	HIS160
C	THR161

site_id	CC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 208

Chain	Residue
C	PHE34
C	ASN36
C	HOH213
C	HOH222

site_id	DC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 C 209

Chain	Residue
B	SER195
C	GLN85
C	ILE87
C	LYS88
C	MG202
C	HOH233

site_id	DC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 202

Chain	Residue
D	MSE84
D	ILE87
D	PRO89
D	PO4209
D	HOH210

site_id	DC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG D 203

Chain	Residue
D	TYR66
D	ARG196

site_id	DC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG D 204

Chain	Residue
D	PRO70
D	GLY71
D	GLY72
D	SER101

site_id	DC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL D 205

Chain	Residue
D	SER101
D	MSE102
D	HIS126

site_id	DC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG D 206

Chain	Residue
D	ASN176
D	PHE177
D	MSE178

site_id	DC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL D 207

Chain	Residue
D	LYS184
D	HIS191
D	VAL192

site_id	DC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG D 208

Chain	Residue
D	THR161
D	ALA185

site_id	DC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 D 209

Chain	Residue
D	GLN85
D	ILE87
D	LYS88
D	ASP90
D	MG202
D	HOH346

site_id	EC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG E 202

Chain	Residue
E	MSE84
E	ILE87
E	PRO89
E	PO4210
E	HOH223

site_id	EC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG E 203

Chain	Residue
E	TYR64
E	TYR66
E	ARG196

site_id	EC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEG E 204

Chain	Residue
E	SER101
E	SER104
E	ILE125
E	HIS126
E	PRO128
E	LEU153
E	HOH311

site_id	EC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG E 205

Chain	Residue
E	GLU38
E	PRO70
E	SER101
E	LEU129

site_id	EC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG E 206

Chain	Residue
E	ASN176
E	PHE177
E	HOH232

site_id	EC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL E 207

Chain	Residue
E	THR161
E	GLY162
E	ALA185
E	GLY187
E	HOH319

site_id	EC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL E 208

Chain	Residue
E	ASN36
E	HOH214
E	HOH220

site_id	EC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL E 209

Chain	Residue
E	HIS160

site_id	EC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 E 210

Chain	Residue
C	GLU197
E	GLN85
E	ILE87
E	ASP90
E	MG202
E	HOH211
E	HOH283

site_id	FC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG F 202

Chain	Residue
F	MSE84
F	ILE87
F	PRO89
F	PO4208

site_id	FC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG F 203

Chain	Residue
F	GLY72
F	SER101
F	HOH224
F	HOH248

site_id	FC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEG F 204

Chain	Residue
F	SER101
F	SER104
F	ILE125
F	HIS126
F	PRO128
F	LEU157
F	HOH224

site_id	FC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL F 205

Chain	Residue
F	ASN176
F	PHE177
F	MSE178
F	GLU182

site_id	FC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO F 206

Chain	Residue
F	THR161
F	ALA185

site_id	FC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG F 207

Chain	Residue
F	TYR66
F	ARG196

site_id	FC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 F 208

Chain	Residue
E	GLU197
F	GLN85
F	ILE87
F	LYS88
F	ASP90
F	MG202

site_id	FC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG G 202

Chain	Residue
G	MSE84
G	ILE87
G	PRO89
G	PO4211
G	HOH233

site_id	FC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG G 203

Chain	Residue
G	ILE32
G	TYR66
G	ARG196

site_id	GC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEG G 204

Chain	Residue
G	SER101
G	MSE102
G	ILE125
G	HIS126
G	GLN127
G	PRO128
G	LEU157

site_id	GC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PEG G 205

Chain	Residue
G	PRO70
G	GLY71
G	GLY72
G	SER101
G	LEU129
G	HOH262

site_id	GC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG G 206

Chain	Residue
G	ASN176
G	PHE177
G	MSE178

site_id	GC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 G 207

Chain	Residue
G	LYS184
G	HIS191
G	VAL192

site_id	GC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO G 208

Chain	Residue
G	LYS112

site_id	GC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG G 209

Chain	Residue
E	ASP181
G	THR161
G	GLN163
G	ALA185

site_id	GC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL G 210

Chain	Residue
B	ASN45
G	HOH223

site_id	GC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 G 211

Chain	Residue
A	HOH262
G	GLN85
G	ILE87
G	LYS88
G	PRO89
G	ASP90
G	MG202

Functional Information from PROSITE/UniProt

site_id	PS00381
Number of Residues	12
Details	CLP_PROTEASE_SER Endopeptidase Clp serine active site. TicIGlAASMGS

Chain	Residue	Details
A	THR93-SER104

site_id	PS00382
Number of Residues	14
Details	CLP_PROTEASE_HIS Endopeptidase Clp histidine active site. RyslPssqIMIHQP

Chain	Residue	Details
A	ARG115-PRO128

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	7
Details	ACT_SITE: Nucleophile => ECO:0000255\|HAMAP-Rule:MF_00444

Chain	Residue	Details
A	SER101
B	SER101
C	SER101
D	SER101
E	SER101
F	SER101
G	SER101

site_id	SWS_FT_FI2
Number of Residues	7
Details	ACT_SITE: ACT_SITE => ECO:0000255\|HAMAP-Rule:MF_00444

Chain	Residue	Details
A	HIS126
B	HIS126
C	HIS126
D	HIS126
E	HIS126
F	HIS126
G	HIS126

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