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5VYY

Structure of human Hsp90-alpha bound to resorcinylic inhibitor BnIm

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 9QY A 301
ChainResidue
AASN51
AHOH431
AHOH451
AALA55
AASP93
AMET98
AASN106
APHE138
ATHR184
AVAL186
AHOH427

site_idAC2
Number of Residues8
Detailsbinding site for residue FMT A 302
ChainResidue
AASN51
AGLY135
AVAL136
AGLY137
APHE138
AHOH439
AHOH503
AHOH523

site_idAC3
Number of Residues3
Detailsbinding site for residue FMT A 303
ChainResidue
AASN35
ATHR36
AHOH511

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO A 304
ChainResidue
AGLN85
AGLU223
AHOH528

site_idAC5
Number of Residues6
Detailsbinding site for residue MG A 305
ChainResidue
AALA27
ASER31
AALA166
AHOH404
AHOH477
AHOH544

site_idAC6
Number of Residues6
Detailsbinding site for residue NA A 306
ChainResidue
AASP193
AASP193
AGLN194
AGLN194
AHOH428
AHOH428

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

247536

PDB entries from 2026-01-14

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