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2BRE

STRUCTURE OF A HSP90 INHIBITOR BOUND TO THE N-TERMINUS OF YEAST HSP90.

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 Residues13
DetailsBINDING SITE FOR RESIDUE KJ2 A1214
ChainResidue
AASN37
ATHR171
ALEU173
AHOH2101
AHOH2120
AASP40
AALA41
AASP79
AILE82
AGLY83
AMET84
AGLY121
APHE124

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE KJ2 B1220
ChainResidue
BASN37
BASP40
BALA41
BASP79
BILE82
BGLY83
BMET84
BGLY121
BPHE124
BTHR171
BLEU173
BHOH2057
BHOH2134

Functional Information from PROSITE/UniProt
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE
ChainResidueDetails
ATYR24-GLU33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:16625188, ECO:0007744|PDB:2CG9
ChainResidueDetails
AGLU33
BLYS98
BSER99
BTHR171
AMET84
AASN92
ALYS98
ASER99
ATHR171
BGLU33
BMET84
BASN92

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16625188, ECO:0000269|PubMed:9230303, ECO:0007744|PDB:1AM1, ECO:0007744|PDB:1AMW, ECO:0007744|PDB:2CG9, ECO:0007744|PDB:2WEP
ChainResidueDetails
AASN37
AASP79
AGLN119
BASN37
BASP79
BGLN119

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PDB entries from 2024-07-10

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