Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6W9T

Crystal structure of Neisseria meningitidis ClpP protease complex with small molecule activator ACP1-06

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	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	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	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	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	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	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	0051117	molecular_function	ATPase binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue K A 301

Chain	Residue
A	MET85
A	ILE88
A	PRO90
A	HOH431
A	HOH451

site_id	AC2
Number of Residues	6
Details	binding site for residue K B 301

Chain	Residue
B	HOH445
B	HOH473
B	MET85
B	ILE88
B	PRO90
B	HOH405

site_id	AC3
Number of Residues	5
Details	binding site for residue K C 301

Chain	Residue
C	MET85
C	ILE88
C	PRO90
C	HOH416
C	HOH467

site_id	AC4
Number of Residues	4
Details	binding site for residue K D 301

Chain	Residue
D	MET85
D	ILE88
D	PRO90
D	HOH449

site_id	AC5
Number of Residues	6
Details	binding site for residue K E 301

Chain	Residue
E	MET85
E	ILE88
E	PRO90
E	HOH415
E	HOH473
E	HOH474

site_id	AC6
Number of Residues	15
Details	binding site for residue KHS F 301

Chain	Residue
E	LEU53
E	GLU56
E	SER57
F	GLU31
F	ILE33
F	ASP63
F	PHE65
F	TYR67
F	SER93
F	LYS115
F	PHE117
F	ARG199
F	HOH402
F	HOH425
F	HOH480

site_id	AC7
Number of Residues	6
Details	binding site for residue K F 302

Chain	Residue
F	MET85
F	ILE88
F	PRO90
F	HOH411
F	HOH447
F	HOH484

site_id	AC8
Number of Residues	6
Details	binding site for residue K G 301

Chain	Residue
G	MET85
G	ILE88
G	PRO90
G	HOH428
G	HOH466
G	HOH495

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	THR94-ALA105

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

Chain	Residue	Details
A	ARG116-PRO129

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	SER102
B	SER102
C	SER102
D	SER102
E	SER102
F	SER102
G	SER102

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

Chain	Residue	Details
A	HIS127
B	HIS127
C	HIS127
D	HIS127
E	HIS127
F	HIS127
G	HIS127

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