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6CYG

Hsp90-alpha N-domain bound to NEOCA

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 Residues16
Detailsbinding site for residue N5O A 301
ChainResidue
AASN51
ATHR184
AHOH401
AHOH424
AHOH479
AHOH559
AHOH572
AHOH603
AALA55
AASP93
AMET98
AASN106
ASER113
AGLY135
AVAL136
ATYR139

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 302
ChainResidue
AGLU62
ALYS69
AILE96
AASN155

site_idAC3
Number of Residues4
Detailsbinding site for residue MG B 301
ChainResidue
BILE110
BSER113
BHOH602
BHOH691

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

239149

PDB entries from 2025-07-23

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