8A8V

Mycobacterium tuberculosis ClpC1 hexamer structure bound to the natural product antibiotic Cyclomarin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005886	cellular_component	plasma membrane
A	0006457	biological_process	protein folding
A	0016887	molecular_function	ATP hydrolysis activity
A	0042803	molecular_function	protein homodimerization activity
A	0044183	molecular_function	protein folding chaperone
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005886	cellular_component	plasma membrane
B	0006457	biological_process	protein folding
B	0016887	molecular_function	ATP hydrolysis activity
B	0042803	molecular_function	protein homodimerization activity
B	0044183	molecular_function	protein folding chaperone
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005886	cellular_component	plasma membrane
C	0006457	biological_process	protein folding
C	0016887	molecular_function	ATP hydrolysis activity
C	0042803	molecular_function	protein homodimerization activity
C	0044183	molecular_function	protein folding chaperone
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005886	cellular_component	plasma membrane
D	0006457	biological_process	protein folding
D	0016887	molecular_function	ATP hydrolysis activity
D	0042803	molecular_function	protein homodimerization activity
D	0044183	molecular_function	protein folding chaperone
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005886	cellular_component	plasma membrane
E	0006457	biological_process	protein folding
E	0016887	molecular_function	ATP hydrolysis activity
E	0042803	molecular_function	protein homodimerization activity
E	0044183	molecular_function	protein folding chaperone
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005886	cellular_component	plasma membrane
F	0006457	biological_process	protein folding
F	0016887	molecular_function	ATP hydrolysis activity
F	0042803	molecular_function	protein homodimerization activity
F	0044183	molecular_function	protein folding chaperone

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASP303-GLY315

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	84
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	573
Details	Region: {"description":"II"}

Chain

Residue

Details

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