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2XJJ

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
B0005524molecular_functionATP binding
B0006457biological_processprotein folding
B0016887molecular_functionATP hydrolysis activity
B0051082molecular_functionunfolded protein binding
B0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1224
ChainResidue
AASN106
AGLY135
AVAL136
AGLY137
APHE138
ATYR139
AHOH2151
AHOH2257

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 1224
ChainResidue
BLYS112
BGLY135
BVAL136
BGLY137
BPHE138
BL811225
BHOH2186
BHOH2254
BHOH2255
BASN106

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE L81 A 1225
ChainResidue
ALEU48
AASN51
AASP54
AALA55
ALYS58
AASP93
AILE96
AGLY97
AMET98
APHE138
ATHR184
AVAL186
AHOH2132
AHOH2258

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE L81 B 1225
ChainResidue
BASN51
BASP54
BALA55
BLYS58
BASP93
BILE96
BGLY97
BMET98
BPHE138
BTHR184
BVAL186
BGOL1224
BHOH2068
BHOH2140

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 Residues6
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07901","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

251174

PDB entries from 2026-03-25

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