Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2CBY

Crystal structure of the ATP-dependent Clp Protease proteolytic subunit 1 (ClpP1) from Mycobacterium tuberculosis

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	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006508	biological_process	proteolysis
A	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
A	0008233	molecular_function	peptidase activity
A	0008236	molecular_function	serine-type peptidase activity
A	0009368	cellular_component	endopeptidase Clp complex
A	0016787	molecular_function	hydrolase activity
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	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006508	biological_process	proteolysis
B	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
B	0008233	molecular_function	peptidase activity
B	0008236	molecular_function	serine-type peptidase activity
B	0009368	cellular_component	endopeptidase Clp complex
B	0016787	molecular_function	hydrolase activity
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	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0006508	biological_process	proteolysis
C	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
C	0008233	molecular_function	peptidase activity
C	0008236	molecular_function	serine-type peptidase activity
C	0009368	cellular_component	endopeptidase Clp complex
C	0016787	molecular_function	hydrolase activity
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	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006508	biological_process	proteolysis
D	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
D	0008233	molecular_function	peptidase activity
D	0008236	molecular_function	serine-type peptidase activity
D	0009368	cellular_component	endopeptidase Clp complex
D	0016787	molecular_function	hydrolase activity
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	0005829	cellular_component	cytosol
E	0005886	cellular_component	plasma membrane
E	0006508	biological_process	proteolysis
E	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
E	0008233	molecular_function	peptidase activity
E	0008236	molecular_function	serine-type peptidase activity
E	0009368	cellular_component	endopeptidase Clp complex
E	0016787	molecular_function	hydrolase activity
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	0005829	cellular_component	cytosol
F	0005886	cellular_component	plasma membrane
F	0006508	biological_process	proteolysis
F	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
F	0008233	molecular_function	peptidase activity
F	0008236	molecular_function	serine-type peptidase activity
F	0009368	cellular_component	endopeptidase Clp complex
F	0016787	molecular_function	hydrolase activity
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	0005829	cellular_component	cytosol
G	0005886	cellular_component	plasma membrane
G	0006508	biological_process	proteolysis
G	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
G	0008233	molecular_function	peptidase activity
G	0008236	molecular_function	serine-type peptidase activity
G	0009368	cellular_component	endopeptidase Clp complex
G	0016787	molecular_function	hydrolase activity
G	0051117	molecular_function	ATPase binding

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ARG112-PRO125

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	SER98
B	SER98
C	SER98
D	SER98
E	SER98
F	SER98
G	SER98

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

Chain	Residue	Details
A	HIS123
B	HIS123
C	HIS123
D	HIS123
E	HIS123
F	HIS123
G	HIS123

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1tyf

Chain	Residue	Details
A	SER98
A	ASP172
A	HIS123
A	MET99
A	GLY69

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1tyf

Chain	Residue	Details
B	SER98
B	ASP172
B	HIS123
B	MET99
B	GLY69

site_id	CSA3
Number of Residues	5
Details	Annotated By Reference To The Literature 1tyf

Chain	Residue	Details
C	SER98
C	ASP172
C	HIS123
C	MET99
C	GLY69

site_id	CSA4
Number of Residues	5
Details	Annotated By Reference To The Literature 1tyf

Chain	Residue	Details
D	SER98
D	ASP172
D	HIS123
D	MET99
D	GLY69

site_id	CSA5
Number of Residues	5
Details	Annotated By Reference To The Literature 1tyf

Chain	Residue	Details
E	SER98
E	ASP172
E	HIS123
E	MET99
E	GLY69

site_id	CSA6
Number of Residues	5
Details	Annotated By Reference To The Literature 1tyf

Chain	Residue	Details
F	SER98
F	ASP172
F	HIS123
F	MET99
F	GLY69

site_id	CSA7
Number of Residues	5
Details	Annotated By Reference To The Literature 1tyf

Chain	Residue	Details
G	SER98
G	ASP172
G	HIS123
G	MET99
G	GLY69

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