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2BT0

Novel, potent small molecule inhibitors of the molecular chaperone Hsp90 discovered through structure-based design

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 Residues15
DetailsBINDING SITE FOR RESIDUE CT5 A1224
ChainResidue
AASN51
AGLY108
APHE138
ATHR184
AVAL186
AHOH2120
AHOH2240
ASER52
AASP54
AALA55
ALYS58
AASP93
AILE96
AGLY97
ALEU107

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE CT5 B1224
ChainResidue
BASN51
BSER52
BALA55
BASP93
BILE96
BGLY97
BMET98
BASN106
BLEU107
BPHE138
BTHR184
BVAL186
BHOH2073
BHOH2129
BHOH2132
BHOH2247

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:
ChainResidueDetails
ASER52
ATHR94
ATYR139
BSER52
BTHR94
BTYR139

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER113
BSER113

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by PRKDC => ECO:0000269|PubMed:2507541
ChainResidueDetails
AGLN6
AGLN8
BGLN6
BGLN8

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07901
ChainResidueDetails
AILE59
AGLN85
BILE59
BGLN85

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:2492519, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
AASP232
BASP232

229183

PDB entries from 2024-12-18

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