Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1TG6

Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004175	molecular_function	endopeptidase activity
A	0004176	molecular_function	ATP-dependent peptidase activity
A	0004252	molecular_function	serine-type endopeptidase activity
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
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	0033619	biological_process	membrane protein proteolysis
A	0035694	biological_process	mitochondrial protein catabolic process
A	0042802	molecular_function	identical protein binding
A	0051117	molecular_function	ATPase binding
A	0051603	biological_process	proteolysis involved in protein catabolic process
B	0004175	molecular_function	endopeptidase activity
B	0004176	molecular_function	ATP-dependent peptidase activity
B	0004252	molecular_function	serine-type endopeptidase activity
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
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	0033619	biological_process	membrane protein proteolysis
B	0035694	biological_process	mitochondrial protein catabolic process
B	0042802	molecular_function	identical protein binding
B	0051117	molecular_function	ATPase binding
B	0051603	biological_process	proteolysis involved in protein catabolic process
C	0004175	molecular_function	endopeptidase activity
C	0004176	molecular_function	ATP-dependent peptidase activity
C	0004252	molecular_function	serine-type endopeptidase activity
C	0005515	molecular_function	protein binding
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
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	0033619	biological_process	membrane protein proteolysis
C	0035694	biological_process	mitochondrial protein catabolic process
C	0042802	molecular_function	identical protein binding
C	0051117	molecular_function	ATPase binding
C	0051603	biological_process	proteolysis involved in protein catabolic process
D	0004175	molecular_function	endopeptidase activity
D	0004176	molecular_function	ATP-dependent peptidase activity
D	0004252	molecular_function	serine-type endopeptidase activity
D	0005515	molecular_function	protein binding
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
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	0033619	biological_process	membrane protein proteolysis
D	0035694	biological_process	mitochondrial protein catabolic process
D	0042802	molecular_function	identical protein binding
D	0051117	molecular_function	ATPase binding
D	0051603	biological_process	proteolysis involved in protein catabolic process
E	0004175	molecular_function	endopeptidase activity
E	0004176	molecular_function	ATP-dependent peptidase activity
E	0004252	molecular_function	serine-type endopeptidase activity
E	0005515	molecular_function	protein binding
E	0005739	cellular_component	mitochondrion
E	0005759	cellular_component	mitochondrial matrix
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	0033619	biological_process	membrane protein proteolysis
E	0035694	biological_process	mitochondrial protein catabolic process
E	0042802	molecular_function	identical protein binding
E	0051117	molecular_function	ATPase binding
E	0051603	biological_process	proteolysis involved in protein catabolic process
F	0004175	molecular_function	endopeptidase activity
F	0004176	molecular_function	ATP-dependent peptidase activity
F	0004252	molecular_function	serine-type endopeptidase activity
F	0005515	molecular_function	protein binding
F	0005739	cellular_component	mitochondrion
F	0005759	cellular_component	mitochondrial matrix
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	0033619	biological_process	membrane protein proteolysis
F	0035694	biological_process	mitochondrial protein catabolic process
F	0042802	molecular_function	identical protein binding
F	0051117	molecular_function	ATPase binding
F	0051603	biological_process	proteolysis involved in protein catabolic process
G	0004175	molecular_function	endopeptidase activity
G	0004176	molecular_function	ATP-dependent peptidase activity
G	0004252	molecular_function	serine-type endopeptidase activity
G	0005515	molecular_function	protein binding
G	0005739	cellular_component	mitochondrion
G	0005759	cellular_component	mitochondrial matrix
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	0033619	biological_process	membrane protein proteolysis
G	0035694	biological_process	mitochondrial protein catabolic process
G	0042802	molecular_function	identical protein binding
G	0051117	molecular_function	ATPase binding
G	0051603	biological_process	proteolysis involved in protein catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DIO A 800

Chain	Residue
A	TYR62
A	VAL92
A	LEU114
G	LEU48
G	THR79
G	TYR82

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DIO B 801

Chain	Residue
C	TRP90
C	VAL92
C	LEU114
B	LEU48
B	TYR82
C	TYR62

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DIO D 802

Chain	Residue
C	LEU48
D	TYR62
D	TRP90
D	LEU114

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE DIO E 803

Chain	Residue
D	SER41
D	HOH1144
D	HOH1224
E	CYS30
E	MET32
E	TYR62
E	ASN64

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DIO F 804

Chain	Residue
E	LEU48
F	TYR62
F	TRP90

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DIO G 805

Chain	Residue
F	LEU48
F	TYR82
G	TYR62
G	TRP90
G	VAL92

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 900

Chain	Residue
A	CYS30
A	MET32
A	TYR62
A	HOH928
G	SER41

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO B 901

Chain	Residue
A	SER41
B	MET32

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO B 902

Chain	Residue
A	TYR82
B	TYR62
B	TRP90

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 903

Chain	Residue
B	SER41
B	HOH1061
C	CYS30
C	MET32

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO C 904

Chain	Residue
C	SER41
D	CYS30

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 905

Chain	Residue
D	TYR82
E	TYR62
E	TRP90
E	VAL92

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO F 906

Chain	Residue
E	HOH1091
F	CYS30
F	TYR62

site_id	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO G 907

Chain	Residue
G	HIS60
G	TYR62

site_id	BC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE FME D 1100

Chain	Residue
A	PRO66
A	GLY67
A	GLY68
A	VAL70
A	SER97
A	MET98
A	HIS122
A	GLN123
A	PRO124
A	LEU149
D	HOH1153

site_id	BC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE FME D 1101

Chain	Residue
B	GLY67
B	GLY68
B	VAL70
B	SER97
B	MET98
B	HIS122
B	GLN123
B	PRO124
B	LEU149
D	HOH1229

site_id	BC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE FME D 1102

Chain	Residue
C	GLY67
C	GLY68
C	VAL70
C	SER97
C	MET98
C	HIS122
C	GLN123
C	PRO124
C	LEU149
D	HOH1117

site_id	BC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE FME D 1103

Chain	Residue
D	GLY67
D	GLY68
D	VAL70
D	SER97
D	MET98
D	HIS122
D	GLN123
D	PRO124
D	LEU149
D	HOH1205
D	HOH1208

site_id	CC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FME D 1104

Chain	Residue
E	GLY68
E	VAL70
E	SER97
E	MET98
E	HIS122
E	PRO124
E	LEU149
E	GLY67

site_id	CC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FME D 1105

Chain	Residue
D	HOH1107
F	PRO66
F	GLY68
F	SER97
F	MET98
F	HIS122
F	PRO124
F	HOH1060
F	HOH1122

site_id	CC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE FME D 1106

Chain	Residue
D	HOH1137
G	GLY67
G	GLY68
G	VAL70
G	SER97
G	MET98
G	HIS122
G	PRO124
G	LEU149
G	HOH1008

site_id	CC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL B 1000

Chain	Residue
A	GLU141
A	LEU145
A	HOH931
B	ARG118
B	TYR173
B	MET174
B	SER175
B	HOH1013
B	HOH1021
B	HOH1024

site_id	CC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL B 1001

Chain	Residue
B	GLU141
B	LEU145
B	HOH1020
B	HOH1023
B	HOH1029
C	ARG118
C	TYR173
C	MET174
C	SER175
C	HOH1027

site_id	CC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL C 1002

Chain	Residue
C	GLU141
C	LEU145
C	HOH1047
C	HOH1059
C	HOH1066
D	ARG118
D	TYR173
D	MET174
D	SER175
D	HOH1140

site_id	CC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL D 1003

Chain	Residue
D	GLU141
D	LYS144
D	HOH1113
D	HOH1131
D	HOH1133
D	HOH1162
D	HOH1219
E	ARG118
E	TYR173
E	SER175

site_id	CC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL E 1004

Chain	Residue
E	GLU141
E	LEU145
E	HOH1043
E	HOH1090
F	ARG118
F	TYR173
F	MET174
F	SER175
F	HOH1056
F	HOH1065

site_id	CC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL F 1005

Chain	Residue
F	GLU141
F	LYS144
F	HOH1082
G	ARG118
G	TYR173
G	SER175
G	HOH959
G	HOH971

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	THR89-SER100

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

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:0000269\|PubMed:11923310

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:0000250

Chain	Residue	Details
A	HIS122
B	HIS122
C	HIS122
D	HIS122
E	HIS122
F	HIS122
G	HIS122

site_id	SWS_FT_FI3
Number of Residues	7
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:O88696

Chain	Residue	Details
A	LYS144
B	LYS144
C	LYS144
D	LYS144
E	LYS144
F	LYS144
G	LYS144

site_id	SWS_FT_FI4
Number of Residues	7
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS155
B	LYS155
C	LYS155
D	LYS155
E	LYS155
F	LYS155
G	LYS155

Catalytic Information from CSA

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

Chain	Residue	Details
A	MET98
A	SER97
A	GLY68
A	HIS122
A	ASP171

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

Chain	Residue	Details
B	MET98
B	SER97
B	GLY68
B	HIS122
B	ASP171

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

Chain	Residue	Details
C	MET98
C	SER97
C	GLY68
C	HIS122
C	ASP171

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

Chain	Residue	Details
D	MET98
D	SER97
D	GLY68
D	HIS122
D	ASP171

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

Chain	Residue	Details
E	MET98
E	SER97
E	GLY68
E	HIS122
E	ASP171

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

Chain	Residue	Details
F	MET98
F	SER97
F	GLY68
F	HIS122
F	ASP171

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

Chain	Residue	Details
G	MET98
G	SER97
G	GLY68
G	HIS122
G	ASP171

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)