Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6W22

ClpA Engaged1 State bound to RepA-GFP (ClpA Focused Refinement)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004176	molecular_function	ATP-dependent peptidase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006508	biological_process	proteolysis
A	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
A	0006979	biological_process	response to oxidative stress
A	0016887	molecular_function	ATP hydrolysis activity
A	0034605	biological_process	cellular response to heat
A	0043335	biological_process	protein unfolding
B	0004176	molecular_function	ATP-dependent peptidase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006508	biological_process	proteolysis
B	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
B	0006979	biological_process	response to oxidative stress
B	0016887	molecular_function	ATP hydrolysis activity
B	0034605	biological_process	cellular response to heat
B	0043335	biological_process	protein unfolding
C	0004176	molecular_function	ATP-dependent peptidase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006508	biological_process	proteolysis
C	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
C	0006979	biological_process	response to oxidative stress
C	0016887	molecular_function	ATP hydrolysis activity
C	0034605	biological_process	cellular response to heat
C	0043335	biological_process	protein unfolding
D	0004176	molecular_function	ATP-dependent peptidase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006508	biological_process	proteolysis
D	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
D	0006979	biological_process	response to oxidative stress
D	0016887	molecular_function	ATP hydrolysis activity
D	0034605	biological_process	cellular response to heat
D	0043335	biological_process	protein unfolding
E	0004176	molecular_function	ATP-dependent peptidase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006508	biological_process	proteolysis
E	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
E	0006979	biological_process	response to oxidative stress
E	0016887	molecular_function	ATP hydrolysis activity
E	0034605	biological_process	cellular response to heat
E	0043335	biological_process	protein unfolding
F	0004176	molecular_function	ATP-dependent peptidase activity
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006508	biological_process	proteolysis
F	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
F	0006979	biological_process	response to oxidative stress
F	0016887	molecular_function	ATP hydrolysis activity
F	0034605	biological_process	cellular response to heat
F	0043335	biological_process	protein unfolding

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue ATP A 801

Chain	Residue
A	LEU188
A	LEU361
A	PRO395
F	ARG206
A	ARG191
A	SER216
A	GLY217
A	GLY219
A	LYS220
A	THR221
A	ALA222
A	ILE357

site_id	AC2
Number of Residues	15
Details	binding site for residue ADP A 802

Chain	Residue
A	LEU459
A	VAL460
A	PHE461
A	PRO496
A	THR497
A	GLY498
A	VAL499
A	GLY500
A	LYS501
A	THR502
A	GLU503
A	LEU653
A	VAL661
A	ALA701
A	ARG702

site_id	AC3
Number of Residues	15
Details	binding site for residue ATP B 801

Chain	Residue
A	ALA336
A	ARG339
A	ARG340
B	PRO187
B	LEU188
B	ILE189
B	SER216
B	GLY217
B	GLY219
B	LYS220
B	THR221
B	ALA222
B	THR323
B	ILE357
B	PRO395

site_id	AC4
Number of Residues	13
Details	binding site for residue ATP B 802

Chain	Residue
A	ARG643
B	LEU459
B	VAL460
B	PHE461
B	GLY498
B	VAL499
B	GLY500
B	LYS501
B	THR502
B	GLU503
B	GLU565
B	LYS664
B	ARG702

site_id	AC5
Number of Residues	15
Details	binding site for residue ATP C 801

Chain	Residue
B	ARG339
B	ARG340
C	LEU188
C	ILE189
C	SER216
C	GLY217
C	VAL218
C	GLY219
C	LYS220
C	THR221
C	ALA222
C	ILE357
C	PRO395
C	ASP396
C	ILE399

site_id	AC6
Number of Residues	19
Details	binding site for residue ATP C 802

Chain	Residue
B	GLU639
B	ARG643
C	LEU459
C	VAL460
C	PHE461
C	THR497
C	GLY498
C	VAL499
C	GLY500
C	LYS501
C	THR502
C	GLU503
C	GLU565
C	ASN606
C	VAL661
C	LYS664
C	PHE665
C	ALA701
C	ARG702

site_id	AC7
Number of Residues	16
Details	binding site for residue ATP D 801

Chain	Residue
D	LYS220
D	THR221
D	ALA222
D	ILE357
D	LEU361
D	ILE399
C	ARG339
C	ARG340
D	PRO187
D	LEU188
D	ILE189
D	ARG191
D	SER216
D	GLY217
D	VAL218
D	GLY219

site_id	AC8
Number of Residues	18
Details	binding site for residue ATP D 802

Chain	Residue
C	ARG643
D	LEU459
D	VAL460
D	PHE461
D	THR497
D	GLY498
D	VAL499
D	GLY500
D	LYS501
D	THR502
D	GLU503
D	GLU565
D	ASN606
D	VAL661
D	LYS664
D	PHE665
D	ALA701
D	ARG702

site_id	AC9
Number of Residues	13
Details	binding site for residue ADP E 801

Chain	Residue
E	LEU188
E	ILE189
E	ARG191
E	GLU215
E	SER216
E	GLY217
E	GLY219
E	LYS220
E	ILE357
E	LEU361
E	PRO395
E	ASP396
E	ILE399

site_id	AD1
Number of Residues	14
Details	binding site for residue ATP E 802

Chain	Residue
D	ARG643
E	LEU459
E	VAL460
E	PHE461
E	THR497
E	VAL499
E	GLY500
E	LYS501
E	THR502
E	GLU503
E	ASN606
E	VAL661
E	LYS664
E	ARG702

site_id	AD2
Number of Residues	10
Details	binding site for residue ADP F 801

Chain	Residue
E	ARG339
F	GLU215
F	SER216
F	GLY217
F	VAL218
F	GLY219
F	THR221
F	ILE357
F	PRO395
F	ASP396

site_id	AD3
Number of Residues	8
Details	binding site for residue ADP F 802

Chain	Residue
F	VAL460
F	GLY498
F	VAL499
F	GLY500
F	THR502
F	PHE665
F	ALA701
F	ARG702

Functional Information from PROSITE/UniProt

site_id	PS00870
Number of Residues	13
Details	CLPAB_1 Chaperonins clpA/B signature 1. DAANLIKPlLssG

Chain	Residue	Details
A	ASP302-GLY314

site_id	PS00871
Number of Residues	19
Details	CLPAB_2 Chaperonins clpA/B signature 2. RFDmSEYmERhTvSRLiGA

Chain	Residue	Details
A	ARG518-ALA536

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1488
Details	Region: {"description":"I"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1128
Details	Region: {"description":"II"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	84
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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