Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3KTJ

Structure of ClpP in complex with ADEP2 in monoclinic crystal form

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	0042802	molecular_function	identical protein binding
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	0042802	molecular_function	identical protein binding
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	0042802	molecular_function	identical protein binding
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	0042802	molecular_function	identical protein binding
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	0042802	molecular_function	identical protein binding
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	0042802	molecular_function	identical protein binding
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	0042802	molecular_function	identical protein binding
G	0051117	molecular_function	ATPase binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NHE A 501

Chain	Residue
A	SER69
A	ILE70
A	THR71
A	ARG141
A	HOH226
A	HOH328

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NHE B 502

Chain	Residue
B	HOH265
C	MET94
B	ILE70
B	THR71
B	ARG141

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NHE C 503

Chain	Residue
C	SER69
C	ILE70
C	THR71
C	ARG141
C	HOH226
D	MET94

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NHE D 504

Chain	Residue
D	ILE70
D	THR71
D	ARG141
D	HOH274
E	PRO66

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NHE E 505

Chain	Residue
E	SER69
E	ILE70
E	THR71
E	ARG141
E	HOH321
F	MET94

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NHE F 506

Chain	Residue
F	SER69
F	ILE70
F	THR71
F	ARG141
G	PRO66
G	MET94

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NHE G 507

Chain	Residue
G	SER69
G	ILE70
G	THR71
G	ARG141
G	HOH266

site_id	AC8
Number of Residues	13
Details	BINDING SITE FOR CHAIN H OF ACYLDEPSIPEPTIDE 2

Chain	Residue
A	VAL44
A	LEU48
A	THR79
A	PHE82
A	HOH203
B	ASP26
B	ILE28
B	SER60
B	TYR62
B	ILE92
B	TYR112
B	LEU114
H	HOH43

site_id	AC9
Number of Residues	12
Details	BINDING SITE FOR CHAIN I OF ACYLDEPSIPEPTIDE 2

Chain	Residue
A	ASP26
A	ILE28
A	SER60
A	TYR62
A	ILE92
A	TYR112
A	LEU114
G	VAL44
G	LEU48
G	PHE49
G	THR79
G	PHE82

site_id	BC1
Number of Residues	11
Details	BINDING SITE FOR CHAIN J OF ACYLDEPSIPEPTIDE 2

Chain	Residue
E	VAL44
E	LEU48
E	THR79
E	PHE82
E	HOH222
F	ASP26
F	ILE28
F	SER60
F	TYR62
F	ILE92
F	TYR112

site_id	BC2
Number of Residues	14
Details	BINDING SITE FOR CHAIN K OF ACYLDEPSIPEPTIDE 2

Chain	Residue
B	LEU48
B	THR79
B	PHE82
C	LEU23
C	ASP26
C	SER60
C	TYR62
C	ILE92
C	TYR112
C	LEU114
C	LEU189
K	HOH135
K	HOH261
K	HOH300

site_id	BC3
Number of Residues	13
Details	BINDING SITE FOR CHAIN L OF ACYLDEPSIPEPTIDE 2

Chain	Residue
D	LEU114
D	HOH226
L	HOH270
C	VAL44
C	LEU48
C	THR79
C	PHE82
D	LEU23
D	ASP26
D	SER60
D	TYR62
D	ILE92
D	TYR112

site_id	BC4
Number of Residues	15
Details	BINDING SITE FOR CHAIN M OF ACYLDEPSIPEPTIDE 2

Chain	Residue
D	VAL44
D	LEU48
D	THR79
D	PHE82
E	LEU23
E	ASP26
E	ILE28
E	SER60
E	TYR62
E	ILE92
E	TYR112
E	LEU114
E	LEU189
E	HOH201
M	HOH342

site_id	BC5
Number of Residues	10
Details	BINDING SITE FOR CHAIN N OF ACYLDEPSIPEPTIDE 2

Chain	Residue
F	LEU48
F	THR79
F	PHE82
F	HOH211
G	ASP26
G	ILE28
G	TYR62
G	ILE92
G	LEU114
G	LEU189

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	THR89-ALA100

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

Chain	Residue	Details
A	ARG111-PRO124

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	7
Details	ACT_SITE: Nucleophile => ECO:0000255\|HAMAP-Rule:MF_00444, ECO:0000305\|PubMed:22080375

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, ECO:0000305\|PubMed:22080375

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)