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3K98

HSP90 N-terminal domain in complex with (1R)-2-(5-chloro-2,4-dihydroxybenzoyl)-N-ethylisoindoline-1-carboxamide

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 1RC A 901
ChainResidue
ALEU48
ATHR184
AVAL186
AHOH241
AHOH254
AASN51
AALA55
ALYS58
AASP93
AILE96
AGLY97
AMET98
APHE138

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 902
ChainResidue
AGLU199
AGLU200
AARG201
BHIS154
BASN155

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 1RC B 901
ChainResidue
BHOH5
BHOH6
BASN51
BSER52
BASP54
BALA55
BLYS58
BASP93
BILE96
BMET98
BPHE138
BTHR184
BVAL186

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 site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07901","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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