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2YGF

L89V, L93I and V136M Mutant of N-Term HSP90 complexed with Geldanamycin

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 Residues23
DetailsBINDING SITE FOR RESIDUE GDM A 1215
ChainResidue
AASN37
AGLY121
AVAL122
AGLY123
APHE124
AMET136
ATHR171
AHOH2032
AHOH2033
AHOH2035
AHOH2072
AALA38
AHOH2087
AHOH2100
AHOH2146
AHOH2147
AASP40
AALA41
ALYS44
AASP79
AILE82
AASN92
ALYS98

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1216
ChainResidue
AARG65
ALYS69
AGLU71
ATHR210
AHOH2062
AHOH2148

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 Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16625188","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2CG9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16625188","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9230303","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AM1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1AMW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CG9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WEP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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