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1SS8

GroEL

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006457biological_processprotein folding
A0009314biological_processresponse to radiation
A0009408biological_processresponse to heat
A0016020cellular_componentmembrane
A0016853molecular_functionisomerase activity
A0016887molecular_functionATP hydrolysis activity
A0019068biological_processvirion assembly
A0042026biological_processprotein refolding
A0042802molecular_functionidentical protein binding
A0051082molecular_functionunfolded protein binding
A0051085biological_processchaperone cofactor-dependent protein refolding
A0140662molecular_functionATP-dependent protein folding chaperone
A1990220cellular_componentGroEL-GroES complex
B0000287molecular_functionmagnesium ion binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006457biological_processprotein folding
B0009314biological_processresponse to radiation
B0009408biological_processresponse to heat
B0016020cellular_componentmembrane
B0016853molecular_functionisomerase activity
B0016887molecular_functionATP hydrolysis activity
B0019068biological_processvirion assembly
B0042026biological_processprotein refolding
B0042802molecular_functionidentical protein binding
B0051082molecular_functionunfolded protein binding
B0051085biological_processchaperone cofactor-dependent protein refolding
B0140662molecular_functionATP-dependent protein folding chaperone
B1990220cellular_componentGroEL-GroES complex
C0000287molecular_functionmagnesium ion binding
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006457biological_processprotein folding
C0009314biological_processresponse to radiation
C0009408biological_processresponse to heat
C0016020cellular_componentmembrane
C0016853molecular_functionisomerase activity
C0016887molecular_functionATP hydrolysis activity
C0019068biological_processvirion assembly
C0042026biological_processprotein refolding
C0042802molecular_functionidentical protein binding
C0051082molecular_functionunfolded protein binding
C0051085biological_processchaperone cofactor-dependent protein refolding
C0140662molecular_functionATP-dependent protein folding chaperone
C1990220cellular_componentGroEL-GroES complex
D0000287molecular_functionmagnesium ion binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006457biological_processprotein folding
D0009314biological_processresponse to radiation
D0009408biological_processresponse to heat
D0016020cellular_componentmembrane
D0016853molecular_functionisomerase activity
D0016887molecular_functionATP hydrolysis activity
D0019068biological_processvirion assembly
D0042026biological_processprotein refolding
D0042802molecular_functionidentical protein binding
D0051082molecular_functionunfolded protein binding
D0051085biological_processchaperone cofactor-dependent protein refolding
D0140662molecular_functionATP-dependent protein folding chaperone
D1990220cellular_componentGroEL-GroES complex
E0000287molecular_functionmagnesium ion binding
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006457biological_processprotein folding
E0009314biological_processresponse to radiation
E0009408biological_processresponse to heat
E0016020cellular_componentmembrane
E0016853molecular_functionisomerase activity
E0016887molecular_functionATP hydrolysis activity
E0019068biological_processvirion assembly
E0042026biological_processprotein refolding
E0042802molecular_functionidentical protein binding
E0051082molecular_functionunfolded protein binding
E0051085biological_processchaperone cofactor-dependent protein refolding
E0140662molecular_functionATP-dependent protein folding chaperone
E1990220cellular_componentGroEL-GroES complex
F0000287molecular_functionmagnesium ion binding
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0006457biological_processprotein folding
F0009314biological_processresponse to radiation
F0009408biological_processresponse to heat
F0016020cellular_componentmembrane
F0016853molecular_functionisomerase activity
F0016887molecular_functionATP hydrolysis activity
F0019068biological_processvirion assembly
F0042026biological_processprotein refolding
F0042802molecular_functionidentical protein binding
F0051082molecular_functionunfolded protein binding
F0051085biological_processchaperone cofactor-dependent protein refolding
F0140662molecular_functionATP-dependent protein folding chaperone
F1990220cellular_componentGroEL-GroES complex
G0000287molecular_functionmagnesium ion binding
G0005515molecular_functionprotein binding
G0005524molecular_functionATP binding
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0006457biological_processprotein folding
G0009314biological_processresponse to radiation
G0009408biological_processresponse to heat
G0016020cellular_componentmembrane
G0016853molecular_functionisomerase activity
G0016887molecular_functionATP hydrolysis activity
G0019068biological_processvirion assembly
G0042026biological_processprotein refolding
G0042802molecular_functionidentical protein binding
G0051082molecular_functionunfolded protein binding
G0051085biological_processchaperone cofactor-dependent protein refolding
G0140662molecular_functionATP-dependent protein folding chaperone
G1990220cellular_componentGroEL-GroES complex
Functional Information from PROSITE/UniProt
site_idPS00296
Number of Residues12
DetailsCHAPERONINS_CPN60 Chaperonins cpn60 signature. AAVEEGVVaGGG
ChainResidueDetails
AALA405-GLY416

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues35
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00600, ECO:0000269|PubMed:25174333, ECO:0000305|PubMed:14517228, ECO:0000305|PubMed:9285585, ECO:0007744|PDB:1AON, ECO:0007744|PDB:1PCQ, ECO:0007744|PDB:1PF9, ECO:0007744|PDB:3WVL
ChainResidueDetails
ALEU31
BPRO496
CLEU31
CGLY88
CGLY416
CALA480
CPRO496
DLEU31
DGLY88
DGLY416
DALA480
AGLY88
DPRO496
ELEU31
EGLY88
EGLY416
EALA480
EPRO496
FLEU31
FGLY88
FGLY416
FALA480
AGLY416
FPRO496
GLEU31
GGLY88
GGLY416
GALA480
GPRO496
AALA480
APRO496
BLEU31
BGLY88
BGLY416
BALA480

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00600, ECO:0000269|PubMed:25174333, ECO:0000305|PubMed:14517228, ECO:0000305|PubMed:9285585, ECO:0007744|PDB:1AON, ECO:0007744|PDB:1PF9, ECO:0007744|PDB:3WVL
ChainResidueDetails
AASP52
BASP52
CASP52
DASP52
EASP52
FASP52
GASP52

site_idSWS_FT_FI3
Number of Residues35
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122
ChainResidueDetails
AGLY35
BGLU391
CGLY35
CASP52
CALA278
CARG322
CGLU391
DGLY35
DASP52
DALA278
DARG322
AASP52
DGLU391
EGLY35
EASP52
EALA278
EARG322
EGLU391
FGLY35
FASP52
FALA278
FARG322
AALA278
FGLU391
GGLY35
GASP52
GALA278
GARG322
GGLU391
AARG322
AGLU391
BGLY35
BASP52
BALA278
BARG322

site_idSWS_FT_FI4
Number of Residues7
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122
ChainResidueDetails
AARG118
BARG118
CARG118
DARG118
EARG118
FARG118
GARG118

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1q3q
ChainResidueDetails
ATHR90
AASP52
AASP398
ATHR89

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1q3q
ChainResidueDetails
BTHR90
BASP52
BASP398
BTHR89

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1q3q
ChainResidueDetails
CTHR90
CASP52
CASP398
CTHR89

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1q3q
ChainResidueDetails
DTHR90
DASP52
DASP398
DTHR89

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1q3q
ChainResidueDetails
ETHR90
EASP52
EASP398
ETHR89

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1q3q
ChainResidueDetails
FTHR90
FASP52
FASP398
FTHR89

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1q3q
ChainResidueDetails
GTHR90
GASP52
GASP398
GTHR89

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PDB entries from 2024-05-01

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