1IOK

CRYSTAL STRUCTURE OF CHAPERONIN-60 FROM PARACOCCUS DENITRIFICANS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006457	biological_process	protein folding
A	0016853	molecular_function	isomerase activity
A	0042026	biological_process	protein refolding
A	0051082	molecular_function	unfolded protein binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone
B	0000166	molecular_function	nucleotide binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006457	biological_process	protein folding
B	0016853	molecular_function	isomerase activity
B	0042026	biological_process	protein refolding
B	0051082	molecular_function	unfolded protein binding
B	0140662	molecular_function	ATP-dependent protein folding chaperone
C	0000166	molecular_function	nucleotide binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006457	biological_process	protein folding
C	0016853	molecular_function	isomerase activity
C	0042026	biological_process	protein refolding
C	0051082	molecular_function	unfolded protein binding
C	0140662	molecular_function	ATP-dependent protein folding chaperone
D	0000166	molecular_function	nucleotide binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006457	biological_process	protein folding
D	0016853	molecular_function	isomerase activity
D	0042026	biological_process	protein refolding
D	0051082	molecular_function	unfolded protein binding
D	0140662	molecular_function	ATP-dependent protein folding chaperone
E	0000166	molecular_function	nucleotide binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0006457	biological_process	protein folding
E	0016853	molecular_function	isomerase activity
E	0042026	biological_process	protein refolding
E	0051082	molecular_function	unfolded protein binding
E	0140662	molecular_function	ATP-dependent protein folding chaperone
F	0000166	molecular_function	nucleotide binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0006457	biological_process	protein folding
F	0016853	molecular_function	isomerase activity
F	0042026	biological_process	protein refolding
F	0051082	molecular_function	unfolded protein binding
F	0140662	molecular_function	ATP-dependent protein folding chaperone
G	0000166	molecular_function	nucleotide binding
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0006457	biological_process	protein folding
G	0016853	molecular_function	isomerase activity
G	0042026	biological_process	protein refolding
G	0051082	molecular_function	unfolded protein binding
G	0140662	molecular_function	ATP-dependent protein folding chaperone

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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	70
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00600","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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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

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