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3EKO

Dihydroxylphenyl amides as inhibitors of the Hsp90 molecular chaperone

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 Residues11
DetailsBINDING SITE FOR RESIDUE PYU A 901
ChainResidue
AASN51
AHOH904
AHOH925
AALA55
ALYS58
AASP93
AILE96
AGLY97
AMET98
ATHR184
AHOH902

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 902
ChainResidue
AARG201
BGLU62
BLYS69
BHIS154
BHOH1004
BHOH1011
BHOH1047
BHOH1053

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PYU B 901
ChainResidue
BLEU48
BASN51
BALA55
BLYS58
BASP93
BILE96
BGLY97
BMET98
BTHR184
BVAL186
BHOH996
BHOH998
BHOH1029

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
AASP93
APHE138
AASN51
BASP93
BPHE138
BASN51

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS112
BLYS112

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07901
ChainResidueDetails
BLYS58
BLYS84
ALYS58
ALYS84

221051

PDB entries from 2024-06-12

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