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1BYQ

HSP90 N-TERMINAL DOMAIN BOUND TO ADP-MG

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 Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1001
ChainResidue
AASN51
AADP2001
AHOH2289
AHOH2290
AHOH2291

site_idAC2
Number of Residues26
DetailsBINDING SITE FOR RESIDUE ADP A 2001
ChainResidue
AASN106
ALEU107
AVAL136
AGLY137
APHE138
ATHR184
AMG1001
AHOH2003
AHOH2004
AHOH2012
AHOH2014
AHOH2108
AHOH2129
AHOH2140
AHOH2170
AHOH2187
AHOH2253
AHOH2260
AHOH2289
AHOH2290
AHOH2291
AHOH2366
AASN51
AALA55
AASP93
AMET98

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 Residues3
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07901","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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