1OEL

CONFORMATIONAL VARIABILITY IN THE REFINED STRUCTURE OF THE CHAPERONIN GROEL AT 2.8 ANGSTROM RESOLUTION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006457	biological_process	protein folding
A	0009314	biological_process	response to radiation
A	0009408	biological_process	response to heat
A	0016020	cellular_component	membrane
A	0016853	molecular_function	isomerase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0019068	biological_process	virion assembly
A	0042026	biological_process	protein refolding
A	0042802	molecular_function	identical protein binding
A	0051082	molecular_function	unfolded protein binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone
A	1990220	cellular_component	GroEL-GroES complex
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006457	biological_process	protein folding
B	0009314	biological_process	response to radiation
B	0009408	biological_process	response to heat
B	0016020	cellular_component	membrane
B	0016853	molecular_function	isomerase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0019068	biological_process	virion assembly
B	0042026	biological_process	protein refolding
B	0042802	molecular_function	identical protein binding
B	0051082	molecular_function	unfolded protein binding
B	0140662	molecular_function	ATP-dependent protein folding chaperone
B	1990220	cellular_component	GroEL-GroES complex
C	0000166	molecular_function	nucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006457	biological_process	protein folding
C	0009314	biological_process	response to radiation
C	0009408	biological_process	response to heat
C	0016020	cellular_component	membrane
C	0016853	molecular_function	isomerase activity
C	0016887	molecular_function	ATP hydrolysis activity
C	0019068	biological_process	virion assembly
C	0042026	biological_process	protein refolding
C	0042802	molecular_function	identical protein binding
C	0051082	molecular_function	unfolded protein binding
C	0140662	molecular_function	ATP-dependent protein folding chaperone
C	1990220	cellular_component	GroEL-GroES complex
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006457	biological_process	protein folding
D	0009314	biological_process	response to radiation
D	0009408	biological_process	response to heat
D	0016020	cellular_component	membrane
D	0016853	molecular_function	isomerase activity
D	0016887	molecular_function	ATP hydrolysis activity
D	0019068	biological_process	virion assembly
D	0042026	biological_process	protein refolding
D	0042802	molecular_function	identical protein binding
D	0051082	molecular_function	unfolded protein binding
D	0140662	molecular_function	ATP-dependent protein folding chaperone
D	1990220	cellular_component	GroEL-GroES complex
E	0000166	molecular_function	nucleotide binding
E	0000287	molecular_function	magnesium ion binding
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006457	biological_process	protein folding
E	0009314	biological_process	response to radiation
E	0009408	biological_process	response to heat
E	0016020	cellular_component	membrane
E	0016853	molecular_function	isomerase activity
E	0016887	molecular_function	ATP hydrolysis activity
E	0019068	biological_process	virion assembly
E	0042026	biological_process	protein refolding
E	0042802	molecular_function	identical protein binding
E	0051082	molecular_function	unfolded protein binding
E	0140662	molecular_function	ATP-dependent protein folding chaperone
E	1990220	cellular_component	GroEL-GroES complex
F	0000166	molecular_function	nucleotide binding
F	0000287	molecular_function	magnesium ion binding
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006457	biological_process	protein folding
F	0009314	biological_process	response to radiation
F	0009408	biological_process	response to heat
F	0016020	cellular_component	membrane
F	0016853	molecular_function	isomerase activity
F	0016887	molecular_function	ATP hydrolysis activity
F	0019068	biological_process	virion assembly
F	0042026	biological_process	protein refolding
F	0042802	molecular_function	identical protein binding
F	0051082	molecular_function	unfolded protein binding
F	0140662	molecular_function	ATP-dependent protein folding chaperone
F	1990220	cellular_component	GroEL-GroES complex
G	0000166	molecular_function	nucleotide binding
G	0000287	molecular_function	magnesium ion binding
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0006457	biological_process	protein folding
G	0009314	biological_process	response to radiation
G	0009408	biological_process	response to heat
G	0016020	cellular_component	membrane
G	0016853	molecular_function	isomerase activity
G	0016887	molecular_function	ATP hydrolysis activity
G	0019068	biological_process	virion assembly
G	0042026	biological_process	protein refolding
G	0042802	molecular_function	identical protein binding
G	0051082	molecular_function	unfolded protein binding
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. AAVEEGVVaGGG

Chain	Residue	Details
A	ALA405-GLY416

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	77
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00600","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25174333","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14517228","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9285585","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1AON","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PCQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PF9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WVL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00600","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25174333","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14517228","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9285585","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1AON","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PF9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WVL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	35
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	7
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

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

---