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4YKR

Heat Shock Protein 90 Bound to CS302

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 Residues11
Detailsbinding site for residue 4EP A 301
ChainResidue
AASN51
AHOH426
AHOH459
AALA55
AASP93
AILE96
AGLY97
AMET98
APHE138
ATHR184
AVAL186

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 302
ChainResidue
ASER31
ALEU32
AASN35
ATHR36
APRO179
AHOH465

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 303
ChainResidue
AHIS77
AASN79
ASER169
ATHR219
AHOH500

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL A 304
ChainResidue
AASN40
AGLU42
AILE43
AARG46
ALYS209
AHIS210

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

246031

PDB entries from 2025-12-10

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