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2YEF

HSP90 inhibitors and drugs from fragment and virtual screening

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 Residues4
DetailsBINDING SITE FOR RESIDUE MG A 1227
ChainResidue
AASN51
AANP1228
AHOH2101
AHOH2109

site_idAC2
Number of Residues28
DetailsBINDING SITE FOR RESIDUE ANP A 1228
ChainResidue
AASN106
ALEU107
AGLY132
AGLY135
AVAL136
AGLY137
APHE138
ATHR184
AMG1227
AHOH2101
AHOH2103
AHOH2109
AHOH2118
AHOH2254
AHOH2315
AHOH2381
AHOH2382
AHOH2383
AHOH2385
AHOH2386
AHOH2387
AHOH2388
AHOH2389
AGLU47
AASN51
AALA55
AASP93
AMET98

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:
ChainResidueDetails
AASN51
AASP93
APHE138

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS112

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07901
ChainResidueDetails
ALYS58
ALYS84

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:2492519, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER231

223166

PDB entries from 2024-07-31

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