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7V9R

Crystal Structure of the heptameric EcHsp60

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0006457biological_processprotein folding
A0042026biological_processprotein refolding
A0140662molecular_functionATP-dependent protein folding chaperone
B0005524molecular_functionATP binding
B0006457biological_processprotein folding
B0042026biological_processprotein refolding
B0140662molecular_functionATP-dependent protein folding chaperone
C0005524molecular_functionATP binding
C0006457biological_processprotein folding
C0042026biological_processprotein refolding
C0140662molecular_functionATP-dependent protein folding chaperone
D0005524molecular_functionATP binding
D0006457biological_processprotein folding
D0042026biological_processprotein refolding
D0140662molecular_functionATP-dependent protein folding chaperone
E0005524molecular_functionATP binding
E0006457biological_processprotein folding
E0042026biological_processprotein refolding
E0140662molecular_functionATP-dependent protein folding chaperone
F0005524molecular_functionATP binding
F0006457biological_processprotein folding
F0042026biological_processprotein refolding
F0140662molecular_functionATP-dependent protein folding chaperone
G0005524molecular_functionATP binding
G0006457biological_processprotein folding
G0042026biological_processprotein refolding
G0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PROSITE/UniProt
site_idPS00296
Number of Residues12
DetailsCHAPERONINS_CPN60 Chaperonins cpn60 signature. AAVEEGIVpGGG
ChainResidueDetails
AALA430-GLY441

222624

PDB entries from 2024-07-17

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