Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1Y7O

The structure of Streptococcus pneumoniae A153P ClpP

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	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	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	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	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	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	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	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 PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA A 1001

Chain	Residue
A	MSE79
A	ILE82
A	ALA84

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA C 1002

Chain	Residue
C	MSE79
C	ILE82
C	ALA84
D	SER194

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA F 1003

Chain	Residue
A	GLU188
F	ASP85

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA B 1004

Chain	Residue
B	MSE79
B	ILE82
B	ALA84
B	HOH1032

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA G 1005

Chain	Residue
G	MSE79
G	ILE82
G	LYS83
G	ALA84
G	HOH1011

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA C 1006

Chain	Residue
A	ALA51
C	GLU156

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA E 1007

Chain	Residue
E	MSE79
E	ILE82
E	ALA84

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA F 1008

Chain	Residue
F	MSE79
F	ILE82
F	ALA84
F	HOH1010

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	THR88-THR99

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

Chain	Residue	Details
A	ARG110-PRO123

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	7
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00444","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	7
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00444","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1tyf

Chain	Residue	Details
A	ASP172
A	GLY67

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1tyf

Chain	Residue	Details
B	ASP172
B	GLY67

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1tyf

Chain	Residue	Details
C	ASP172
C	GLY67

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1tyf

Chain	Residue	Details
D	ASP172
D	GLY67

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1tyf

Chain	Residue	Details
E	ASP172
E	GLY67

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1tyf

Chain	Residue	Details
F	ASP172
F	GLY67

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1tyf

Chain	Residue	Details
G	ASP172
G	GLY67

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