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4AWQ

Complex of HSP90 ATPase domain with tropane derived inhibitors

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 Residues18
DetailsBINDING SITE FOR RESIDUE 592 B 1224
ChainResidue
BALA21
BLEU107
BILE110
BPHE138
BTYR139
BTRP162
BPHE170
BTHR184
BVAL186
BHOH2007
BPHE22
BGLN23
BASN51
BASP93
BLEU103
BILE104
BASN105
BASN106

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 592 A 1224
ChainResidue
AALA21
APHE22
AGLN23
AASN51
AASP93
AMET98
ALEU103
AILE104
AASN105
AASN106
ALEU107
AILE110
APHE138
ATYR139
ATRP162
APHE170
ATHR184
AVAL186
AHOH2006

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

246031

PDB entries from 2025-12-10

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