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2WER

Yeast Hsp90 N-terminal domain LI-IV mutant with Radicicol

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 RDC A 1215
ChainResidue
AASN37
APHE124
ATHR171
ALEU173
AHOH2071
AHOH2143
AHOH2144
AASP40
AALA41
ALYS44
AASP79
AILE82
AMET84
AASN92
ALEU93

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE RDC B 1215
ChainResidue
BASN37
BASP40
BALA41
BLYS44
BASP79
BILE82
BMET84
BLEU93
BPHE124
BTHR171
BLEU173
BHOH2117
BHOH2138
BHOH2140

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

226707

PDB entries from 2024-10-30

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