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2QG0

HSP90 complexed with A943037

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 Residues19
DetailsBINDING SITE FOR RESIDUE A94 A 2001
ChainResidue
AASN51
AGLY135
AGLY137
APHE138
ATHR184
AHOH2002
AHOH2003
AHOH2010
AHOH2053
AHOH2255
AHOH2262
AASP54
AALA55
ALYS58
AASP93
AILE96
AGLY97
AMET98
AASN106

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE A94 B 2002
ChainResidue
BASN51
BASP54
BALA55
BLYS58
BASP93
BILE96
BGLY97
BMET98
BASN106
BGLY135
BGLY137
BPHE138
BTYR139
BTHR184
BHOH2004
BHOH2006
BHOH2008
BHOH2011
BHOH2050
BHOH2091
BHOH2098

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
AASN51
AASP93
APHE138
BASN51
BASP93
BPHE138

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
ALYS58
ALYS84
BLYS58
BLYS84

218853

PDB entries from 2024-04-24

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