Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1IOK

CRYSTAL STRUCTURE OF CHAPERONIN-60 FROM PARACOCCUS DENITRIFICANS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006457	biological_process	protein folding
A	0009408	biological_process	response to heat
A	0016853	molecular_function	isomerase activity
A	0042026	biological_process	protein refolding
A	0051082	molecular_function	unfolded protein binding
A	0051085	biological_process	chaperone cofactor-dependent protein refolding
A	0140662	molecular_function	ATP-dependent protein folding chaperone
A	1990220	cellular_component	GroEL-GroES complex
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006457	biological_process	protein folding
B	0009408	biological_process	response to heat
B	0016853	molecular_function	isomerase activity
B	0042026	biological_process	protein refolding
B	0051082	molecular_function	unfolded protein binding
B	0051085	biological_process	chaperone cofactor-dependent protein refolding
B	0140662	molecular_function	ATP-dependent protein folding chaperone
B	1990220	cellular_component	GroEL-GroES complex
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006457	biological_process	protein folding
C	0009408	biological_process	response to heat
C	0016853	molecular_function	isomerase activity
C	0042026	biological_process	protein refolding
C	0051082	molecular_function	unfolded protein binding
C	0051085	biological_process	chaperone cofactor-dependent protein refolding
C	0140662	molecular_function	ATP-dependent protein folding chaperone
C	1990220	cellular_component	GroEL-GroES complex
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006457	biological_process	protein folding
D	0009408	biological_process	response to heat
D	0016853	molecular_function	isomerase activity
D	0042026	biological_process	protein refolding
D	0051082	molecular_function	unfolded protein binding
D	0051085	biological_process	chaperone cofactor-dependent protein refolding
D	0140662	molecular_function	ATP-dependent protein folding chaperone
D	1990220	cellular_component	GroEL-GroES complex
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0006457	biological_process	protein folding
E	0009408	biological_process	response to heat
E	0016853	molecular_function	isomerase activity
E	0042026	biological_process	protein refolding
E	0051082	molecular_function	unfolded protein binding
E	0051085	biological_process	chaperone cofactor-dependent protein refolding
E	0140662	molecular_function	ATP-dependent protein folding chaperone
E	1990220	cellular_component	GroEL-GroES complex
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0006457	biological_process	protein folding
F	0009408	biological_process	response to heat
F	0016853	molecular_function	isomerase activity
F	0042026	biological_process	protein refolding
F	0051082	molecular_function	unfolded protein binding
F	0051085	biological_process	chaperone cofactor-dependent protein refolding
F	0140662	molecular_function	ATP-dependent protein folding chaperone
F	1990220	cellular_component	GroEL-GroES complex
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0006457	biological_process	protein folding
G	0009408	biological_process	response to heat
G	0016853	molecular_function	isomerase activity
G	0042026	biological_process	protein refolding
G	0051082	molecular_function	unfolded protein binding
G	0051085	biological_process	chaperone cofactor-dependent protein refolding
G	0140662	molecular_function	ATP-dependent protein folding chaperone
G	1990220	cellular_component	GroEL-GroES complex

Functional Information from PROSITE/UniProt

site_id	PS00296
Number of Residues	12
Details	CHAPERONINS_CPN60 Chaperonins cpn60 signature. AAVQEGIVvGGG

Chain	Residue	Details
A	ALA405-GLY416

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	35
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00600

Chain	Residue	Details
A	THR30
B	ASP496
C	THR30
C	LYS51
C	ASP87
C	GLY415
C	ASP496
D	THR30
D	LYS51
D	ASP87
D	GLY415
A	LYS51
D	ASP496
E	THR30
E	LYS51
E	ASP87
E	GLY415
E	ASP496
F	THR30
F	LYS51
F	ASP87
F	GLY415
A	ASP87
F	ASP496
G	THR30
G	LYS51
G	ASP87
G	GLY415
G	ASP496
A	GLY415
A	ASP496
B	THR30
B	LYS51
B	ASP87
B	GLY415

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
A	THR90
A	ASP52
A	ASP398
A	THR89

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
B	THR90
B	ASP52
B	ASP398
B	THR89

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
C	THR90
C	ASP52
C	ASP398
C	THR89

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
D	THR90
D	ASP52
D	ASP398
D	THR89

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
E	THR90
E	ASP52
E	ASP398
E	THR89

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
F	THR90
F	ASP52
F	ASP398
F	THR89

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1q3q

Chain	Residue	Details
G	THR90
G	ASP52
G	ASP398
G	THR89

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