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3HEK

HSP90 N-terminal domain in complex with 1-{4-[(2R)-1-(5-chloro-2,4-dihydroxybenzoyl)pyrrolidin-2-yl]benzyl}-3,3-difluoropyrrolidinium

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 Residues17
DetailsBINDING SITE FOR RESIDUE BD0 A 901
ChainResidue
AHOH1
AVAL136
APHE138
ATYR139
ATHR184
AVAL186
AHOH235
AHOH250
AHOH309
ALEU48
AASN51
AALA55
AASP93
AMET98
AASN106
ALEU107
AGLY135

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 902
ChainResidue
AARG201
BGLU62
BLYS69
BHIS154
BASN155
BASP156
BHOH240

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE BD0 B 901
ChainResidue
BHOH2
BHOH4
BLEU48
BASN51
BALA55
BASP93
BGLY97
BMET98
BASN106
BLEU107
BGLY135
BVAL136
BPHE138
BTYR139
BTHR184
BVAL186
BHOH241
BHOH265

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

246333

PDB entries from 2025-12-17

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