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2FXS

Yeast HSP82 in complex with the novel HSP90 Inhibitor Radamide

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 Residues19
DetailsBINDING SITE FOR RESIDUE RDA A 1001
ChainResidue
AASN37
APHE124
ATHR171
ALEU173
AHOH1094
AHOH1095
AHOH1180
AHOH1220
AHOH1221
AHOH1230
AHOH1245
AALA41
ALYS44
AASP79
AILE82
AMET84
AASN91
AASN92
ALYS98

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
ALYS73
AASP132
ALEU177
ALYS178
AASP179
AHOH1135

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
ALYS54
AGLN55
ATHR58
AASN141
AHOH1103
AHOH1259

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 303
ChainResidue
ASER25
AGLU183
AARG189
AHOH1032
AHOH1033
AHOH1190
AHOH1218
AHOH1219

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 304
ChainResidue
AGLU149
AASN151
ASER155
APHE156
ATHR157
AHOH1051
AHOH1184

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 305
ChainResidue
ALYS69
AGLN72
AARG174
AHOH1077
AHOH1174

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: BINDING => ECO:0000269|PubMed:16625188, ECO:0007744|PDB:2CG9
ChainResidueDetails
AGLU33
AMET84
AASN92
ALYS98
ASER99
ATHR171

site_idSWS_FT_FI2
Number of Residues3
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

224201

PDB entries from 2024-08-28

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