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3FT8

Structure of HSP90 bound with a noval fragment.

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
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE MOJ A 237
ChainResidue
AALA55
ATYR139
ATRP162
ATHR184
AHOH243
AHOH255
AHOH257
AHOH269
AASP93
AILE96
AGLY97
AMET98
ALEU107
AALA111
AGLY135
APHE138

Functional Information from PROSITE/UniProt
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE
ChainResidueDetails
ATYR38-GLU47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07901","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

244693

PDB entries from 2025-11-12

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