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2XDU

Structure of HSP90 with small molecule inhibitor bound

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 Residues2
DetailsBINDING SITE FOR RESIDUE MG A 1225
ChainResidue
AGLN23
AHOH2007

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS A 1226
ChainResidue
AHIS77
AASN79
ASER169
AHOH2176
AHOH2230

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE LGA A 1227
ChainResidue
AMET98
ATHR184
AMT01228
AHOH2058
AHOH2122
AALA55
AASP93

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MT0 A 1228
ChainResidue
AMET98
APHE138
ATYR139
ATRP162
ALGA1227
AHOH2231

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

240971

PDB entries from 2025-08-27

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