7DFT

Crystal structure of Xanthomonas oryzae 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	0008236	molecular_function	serine-type peptidase activity
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	0008236	molecular_function	serine-type peptidase activity
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	0008236	molecular_function	serine-type peptidase activity
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	0008236	molecular_function	serine-type peptidase activity
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	0008236	molecular_function	serine-type peptidase activity
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	0008236	molecular_function	serine-type peptidase activity
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	0008236	molecular_function	serine-type peptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue CL A 301

Chain	Residue
A	ARG154
F	HIS146
F	ALA147

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

Chain	Residue
A	HIS146
A	ALA147
A	HOH508
F	ARG154

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site_id	AC3
Number of Residues	2
Details	binding site for residue CL A 303

Chain	Residue
A	SER155
A	ASN158

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site_id	AC4
Number of Residues	3
Details	binding site for residue CL B 301

Chain	Residue
B	HIS146
B	ALA147
E	ARG154

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site_id	AC5
Number of Residues	3
Details	binding site for residue CL C 301

Chain	Residue
C	ARG154
D	HIS146
D	ALA147

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site_id	AC6
Number of Residues	3
Details	binding site for residue CL D 301

Chain	Residue
D	GLY21
D	GLU22
E	ARG20

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site_id	AC7
Number of Residues	4
Details	binding site for residue CL E 301

Chain	Residue
B	ARG154
E	HIS146
E	ALA147
E	HOH516

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site_id	AC8
Number of Residues	3
Details	binding site for residue CL G 301

Chain	Residue
G	HIS146
G	ALA147
G	ARG154

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	THR97-ALA108

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

Chain	Residue	Details
A	ARG119-PRO132

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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	SER105
B	SER105
C	SER105
D	SER105
E	SER105
F	SER105
G	SER105

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

Chain	Residue	Details
A	HIS130
B	HIS130
C	HIS130
D	HIS130
E	HIS130
F	HIS130
G	HIS130

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