Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3KTI

Structure of ClpP in complex with ADEP1

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	4
Details	BINDING SITE FOR RESIDUE DMS A 301

Chain	Residue
A	SER97
A	ILE121
A	HIS122
A	LEU153

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NHE A 501

Chain	Residue
A	HOH612
B	MET94
A	SER69
A	ILE70
A	THR71
A	ARG141
A	HOH238

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMS B 302

Chain	Residue
B	ILE121
B	HIS122
B	LEU153

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NHE B 502

Chain	Residue
B	ILE70
B	THR71
B	ARG141
B	HOH403
B	HOH517
C	PRO66
C	MET94

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMS C 303

Chain	Residue
C	ILE121
C	HIS122
C	LEU153

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NHE C 503

Chain	Residue
C	SER69
C	ILE70
C	THR71
C	ARG141
C	HOH214
C	HOH663
D	PRO66

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DMS D 304

Chain	Residue
D	SER97
D	ILE121
D	HIS122
D	LEU153

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NHE D 504

Chain	Residue
D	ILE70
D	THR71
D	ARG141
D	HOH400
E	PRO66
E	MET94

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DMS E 305

Chain	Residue
E	ILE121
E	HIS122

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NHE E 505

Chain	Residue
E	SER69
E	ILE70
E	THR71
E	ARG141
E	HOH409

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMS F 306

Chain	Residue
F	SER97
F	ILE121
F	HIS122

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE NHE F 506

Chain	Residue
F	SER69
F	ILE70
F	THR71
F	ARG141
F	LEU145
F	HOH394
F	HOH492
G	PRO66
G	MET94

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DMS G 307

Chain	Residue
G	ILE121
G	HIS122

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NHE G 507

Chain	Residue
A	PRO66
G	SER69
G	ILE70
G	THR71
G	ARG141

site_id	BC6
Number of Residues	13
Details	BINDING SITE FOR CHAIN H OF ACYLDEPSIPEPTIDE 1

Chain	Residue
A	ALA52
A	THR79
A	PHE82
A	HOH485
B	ARG22
B	ASP26
B	SER60
B	TYR62
B	ILE90
B	ILE92
B	LYS110
B	TYR112
B	LEU189

site_id	BC7
Number of Residues	15
Details	BINDING SITE FOR CHAIN I OF ACYLDEPSIPEPTIDE 1

Chain	Residue
A	ARG22
A	ASP26
A	GLU58
A	SER60
A	TYR62
A	ILE90
A	ILE92
A	LYS110
A	TYR112
A	LEU114
A	LEU189
G	LEU48
G	ALA52
G	THR79
G	PHE82

site_id	BC8
Number of Residues	10
Details	BINDING SITE FOR CHAIN J OF ACYLDEPSIPEPTIDE 1

Chain	Residue
F	TYR62
F	ILE90
F	LYS110
F	TYR112
F	LEU114
F	LEU189
E	THR79
E	PHE82
F	ASP26
F	SER60

site_id	BC9
Number of Residues	12
Details	BINDING SITE FOR CHAIN K OF ACYLDEPSIPEPTIDE 1

Chain	Residue
B	ALA52
B	THR79
B	PHE82
C	ARG22
C	ASP26
C	GLU58
C	SER60
C	TYR62
C	ILE90
C	LYS110
C	TYR112
C	LEU189

site_id	CC1
Number of Residues	13
Details	BINDING SITE FOR CHAIN L OF ACYLDEPSIPEPTIDE 1

Chain	Residue
C	THR79
C	PHE82
D	ARG22
D	ASP26
D	ILE28
D	GLU58
D	SER60
D	TYR62
D	ILE90
D	ILE92
D	TYR112
D	LEU189
D	HOH410

site_id	CC2
Number of Residues	14
Details	BINDING SITE FOR CHAIN M OF ACYLDEPSIPEPTIDE 1

Chain	Residue
D	THR79
D	PHE82
D	HOH236
E	ARG22
E	LEU23
E	ASP26
E	SER60
E	TYR62
E	ILE90
E	ILE92
E	LYS110
E	TYR112
E	LEU114
E	LEU189

site_id	CC3
Number of Residues	15
Details	BINDING SITE FOR CHAIN N OF ACYLDEPSIPEPTIDE 1

Chain	Residue
F	LEU48
F	THR79
F	PHE82
F	HOH238
G	ARG22
G	ASP26
G	ILE28
G	SER60
G	TYR62
G	ILE90
G	TYR112
G	LEU114
G	LEU189
N	HOH420
N	HOH561

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)