Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6QS7

ClpB (DWB and K476C mutant) bound to casein in presence of ATPgammaS - state KC-2A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0009408	biological_process	response to heat
A	0016020	cellular_component	membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0034605	biological_process	cellular response to heat
A	0042026	biological_process	protein refolding
A	0042802	molecular_function	identical protein binding
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0009408	biological_process	response to heat
B	0016020	cellular_component	membrane
B	0016887	molecular_function	ATP hydrolysis activity
B	0034605	biological_process	cellular response to heat
B	0042026	biological_process	protein refolding
B	0042802	molecular_function	identical protein binding
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0009408	biological_process	response to heat
C	0016020	cellular_component	membrane
C	0016887	molecular_function	ATP hydrolysis activity
C	0034605	biological_process	cellular response to heat
C	0042026	biological_process	protein refolding
C	0042802	molecular_function	identical protein binding
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0009408	biological_process	response to heat
D	0016020	cellular_component	membrane
D	0016887	molecular_function	ATP hydrolysis activity
D	0034605	biological_process	cellular response to heat
D	0042026	biological_process	protein refolding
D	0042802	molecular_function	identical protein binding
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0009408	biological_process	response to heat
E	0016020	cellular_component	membrane
E	0016887	molecular_function	ATP hydrolysis activity
E	0034605	biological_process	cellular response to heat
E	0042026	biological_process	protein refolding
E	0042802	molecular_function	identical protein binding
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0009408	biological_process	response to heat
F	0016020	cellular_component	membrane
F	0016887	molecular_function	ATP hydrolysis activity
F	0034605	biological_process	cellular response to heat
F	0042026	biological_process	protein refolding
F	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue AGS A 1001

Chain	Residue
A	ASP178
A	LEU353
A	PRO387
A	MG1002
F	ARG331
A	VAL180
A	ILE181
A	GLY209
A	VAL210
A	GLY211
A	LYS212
A	THR213
A	ALA214

site_id	AC2
Number of Residues	2
Details	binding site for residue MG A 1002

Chain	Residue
A	THR213
A	AGS1001

site_id	AC3
Number of Residues	16
Details	binding site for residue AGS B 1001

Chain	Residue
A	ARG331
A	ARG332
B	ASP178
B	PRO179
B	VAL180
B	ILE181
B	ARG183
B	GLY209
B	GLY211
B	LYS212
B	THR213
B	ALA214
B	ILE349
B	LEU353
B	PRO387
B	MG1003

site_id	AC4
Number of Residues	18
Details	binding site for residue AGS B 1002

Chain	Residue
A	ARG756
B	ARG569
B	VAL570
B	ILE571
B	GLY572
B	THR607
B	GLY608
B	VAL609
B	GLY610
B	LYS611
B	THR612
B	GLU613
B	ASN719
B	ILE774
B	GLN778
B	ARG815
B	LYS818
B	MG1004

site_id	AC5
Number of Residues	2
Details	binding site for residue MG B 1003

Chain	Residue
B	THR213
B	AGS1001

site_id	AC6
Number of Residues	3
Details	binding site for residue MG B 1004

Chain	Residue
B	THR612
B	ASP677
B	AGS1002

site_id	AC7
Number of Residues	15
Details	binding site for residue AGS C 1001

Chain	Residue
B	ARG331
B	ARG332
C	PRO179
C	ILE181
C	ARG183
C	PRO208
C	GLY209
C	GLY211
C	LYS212
C	THR213
C	ALA214
C	ILE349
C	LEU353
C	ILE391
C	MG1003

site_id	AC8
Number of Residues	14
Details	binding site for residue AGS C 1002

Chain	Residue
B	GLU752
B	ARG756
C	ARG569
C	ILE571
C	GLY608
C	VAL609
C	GLY610
C	LYS611
C	THR612
C	GLU613
C	GLN778
C	ARG815
C	LYS818
C	MG1004

site_id	AC9
Number of Residues	2
Details	binding site for residue MG C 1003

Chain	Residue
C	THR213
C	AGS1001

site_id	AD1
Number of Residues	4
Details	binding site for residue MG C 1004

Chain	Residue
C	THR612
C	ASP677
C	THR717
C	AGS1002

site_id	AD2
Number of Residues	14
Details	binding site for residue AGS D 1001

Chain	Residue
D	ILE349
D	LEU353
D	PRO387
D	MG1003
C	ARG331
C	ARG332
D	PRO179
D	ILE181
D	PRO208
D	GLY209
D	VAL210
D	GLY211
D	LYS212
D	THR213

site_id	AD3
Number of Residues	16
Details	binding site for residue AGS D 1002

Chain	Residue
C	ARG756
D	ARG569
D	ILE571
D	THR607
D	GLY608
D	VAL609
D	GLY610
D	LYS611
D	THR612
D	GLU613
D	ILE774
D	GLN778
D	ALA814
D	ARG815
D	LYS818
D	MG1004

site_id	AD4
Number of Residues	2
Details	binding site for residue MG D 1003

Chain	Residue
D	THR213
D	AGS1001

site_id	AD5
Number of Residues	3
Details	binding site for residue MG D 1004

Chain	Residue
D	THR612
D	ASP677
D	AGS1002

site_id	AD6
Number of Residues	14
Details	binding site for residue AGS E 1001

Chain	Residue
D	ARG331
D	ARG332
E	ASP178
E	PRO179
E	VAL180
E	ILE181
E	GLY209
E	VAL210
E	GLY211
E	LYS212
E	THR213
E	ALA214
E	ILE349
E	LEU353

site_id	AD7
Number of Residues	16
Details	binding site for residue AGS E 1002

Chain	Residue
D	ASP695
E	ARG569
E	VAL570
E	ILE571
E	GLY572
E	GLY608
E	VAL609
E	GLY610
E	LYS611
E	THR612
E	GLU613
E	ILE774
E	ALA814
E	ARG815
E	LYS818
E	MG1003

site_id	AD8
Number of Residues	3
Details	binding site for residue MG E 1003

Chain	Residue
E	THR612
E	ASP677
E	AGS1002

site_id	AD9
Number of Residues	18
Details	binding site for residue ADP F 1001

Chain	Residue
E	GLU330
E	ARG331
F	ASP178
F	PRO179
F	VAL180
F	ILE181
F	GLU207
F	PRO208
F	GLY209
F	VAL210
F	GLY211
F	LYS212
F	THR213
F	ALA214
F	ILE349
F	LEU353
F	PRO387
F	ASP388

site_id	AE1
Number of Residues	15
Details	binding site for residue AGS F 1002

Chain	Residue
F	VAL570
F	ILE571
F	PRO606
F	THR607
F	GLY608
F	VAL609
F	GLY610
F	LYS611
F	THR612
F	GLU613
F	ARG631
F	ASP677
F	ILE774
F	ALA814
F	ARG815

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASP294-GLY306

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

Chain	Residue	Details
A	ARG631-ALA649

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING:

Chain	Residue	Details
A	GLY206
E	GLY605
F	GLY206
F	GLY605
A	GLY605
B	GLY206
B	GLY605
C	GLY206
C	GLY605
D	GLY206
D	GLY605
E	GLY206

site_id	SWS_FT_FI2
Number of Residues	18
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:18723842

Chain	Residue	Details
A	LYS96
D	LYS96
D	LYS176
D	LYS640
E	LYS96
E	LYS176
E	LYS640
F	LYS96
F	LYS176
F	LYS640
A	LYS176
A	LYS640
B	LYS96
B	LYS176
B	LYS640
C	LYS96
C	LYS176
C	LYS640

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