Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6HWN

Structure of Thermus thermophilus ClpP in complex with a tripeptide.

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	2
Details	binding site for residue PEG A 301

Chain	Residue
A	GLN159
A	GLU181

site_id	AC2
Number of Residues	4
Details	binding site for residue PEG A 302

Chain	Residue
A	TYR172
A	LEU174
A	GLU178
A	HOH449

site_id	AC3
Number of Residues	4
Details	binding site for residue PEG A 303

Chain	Residue
A	HOH401
A	ASN56
A	ARG110
A	GLY158

site_id	AC4
Number of Residues	4
Details	binding site for residue PEG B 301

Chain	Residue
B	THR157
B	GLU181
B	TYR182
B	PEG302

site_id	AC5
Number of Residues	5
Details	binding site for residue PEG B 302

Chain	Residue
B	LYS108
B	HIS156
B	THR157
B	GLY158
B	PEG301

site_id	AC6
Number of Residues	2
Details	binding site for residue PEG B 303

Chain	Residue
B	TYR172
B	TYR173

site_id	AC7
Number of Residues	7
Details	binding site for residue PEG C 301

Chain	Residue
C	GLN140
C	HOH401
C	HOH423
F	THR157
F	GLY158
F	GLN159
F	GLU181

site_id	AC8
Number of Residues	4
Details	binding site for residue PEG C 302

Chain	Residue
C	LYS108
C	HIS156
C	THR157
C	PEG303

site_id	AC9
Number of Residues	4
Details	binding site for residue PEG C 303

Chain	Residue
C	THR157
C	GLY158
C	GLU181
C	PEG302

site_id	AD1
Number of Residues	4
Details	binding site for residue PEG D 301

Chain	Residue
D	THR157
D	GLY158
D	GLN159
D	GLU181

site_id	AD2
Number of Residues	7
Details	binding site for residue PEG D 302

Chain	Residue
D	ASP78
D	GLN81
D	PHE82
D	HOH428
E	PRO115
E	HIS116
E	THR190

site_id	AD3
Number of Residues	6
Details	binding site for residue PEG D 303

Chain	Residue
D	PRO115
D	SER175
D	ALA176
D	GLN177
D	HOH413
F	LYS166

site_id	AD4
Number of Residues	4
Details	binding site for residue PEG D 304

Chain	Residue
D	LYS108
D	HIS156
D	THR157
D	GLY158

site_id	AD5
Number of Residues	3
Details	binding site for residue PEG E 301

Chain	Residue
E	TYR172
E	TYR173
E	HOH403

site_id	AD6
Number of Residues	4
Details	binding site for residue PEG E 302

Chain	Residue
E	GLN81
E	LYS155
E	HIS156
F	ARG191

site_id	AD7
Number of Residues	2
Details	binding site for residue PEG F 301

Chain	Residue
F	ILE35
F	GLY68

site_id	AD8
Number of Residues	4
Details	binding site for residue PEG G 301

Chain	Residue
G	THR157
G	GLN159
G	GLU181
G	TYR182

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ARG111-PRO124

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

Chain	Residue	Details
A	THR89-ALA100

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	SER97
B	SER97
C	SER97
D	SER97
E	SER97
F	SER97
G	SER97

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

Chain	Residue	Details
A	HIS122
B	HIS122
C	HIS122
D	HIS122
E	HIS122
F	HIS122
G	HIS122

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