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8OXU

Crystal Structure of the Hsp90-LA1011 Complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0006457biological_processprotein folding
A0016887molecular_functionATP hydrolysis activity
A0051082molecular_functionunfolded protein binding
A0140662molecular_functionATP-dependent protein folding chaperone
B0005524molecular_functionATP binding
B0006457biological_processprotein folding
B0016887molecular_functionATP hydrolysis activity
B0051082molecular_functionunfolded protein binding
B0140662molecular_functionATP-dependent protein folding chaperone
C0005524molecular_functionATP binding
C0006457biological_processprotein folding
C0016887molecular_functionATP hydrolysis activity
C0051082molecular_functionunfolded protein binding
C0140662molecular_functionATP-dependent protein folding chaperone
D0005524molecular_functionATP binding
D0006457biological_processprotein folding
D0016887molecular_functionATP hydrolysis activity
D0051082molecular_functionunfolded protein binding
D0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P15108
ChainResidueDetails
ASER657
BSER657
CSER657
DSER657

222415

PDB entries from 2024-07-10

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