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5GGZ

Crystal structure of novel inhibitor bound with Hsp90

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
C0005524molecular_functionATP binding
C0006457biological_processprotein folding
C0016887molecular_functionATP hydrolysis activity
C0051082molecular_functionunfolded protein binding
C0140662molecular_functionATP-dependent protein folding chaperone
D0005524molecular_functionATP binding
D0006457biological_processprotein folding
D0016887molecular_functionATP hydrolysis activity
D0051082molecular_functionunfolded protein binding
D0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue 6TN B 301
ChainResidue
BASN51
BTHR184
BVAL186
BHOH405
BHOH444
BHOH457
DTYR61
BALA55
BLYS58
BASP93
BILE96
BGLY97
BMET98
BLEU107
BPHE138

site_idAC2
Number of Residues11
Detailsbinding site for residue 6TN A 301
ChainResidue
AASN51
AALA55
AASP93
AILE96
AGLY97
APHE138
ATHR184
AVAL186
AHOH409
AHOH438
CTYR61

site_idAC3
Number of Residues11
Detailsbinding site for residue 6TN D 301
ChainResidue
BTYR61
DASN51
DALA55
DASP93
DILE96
DGLY97
DPHE138
DTHR184
DVAL186
DHOH421
DHOH452

site_idAC4
Number of Residues14
Detailsbinding site for residue 6TN C 301
ChainResidue
ATYR61
CASN51
CALA55
CLYS58
CASP93
CILE96
CGLY97
CMET98
CLEU107
CPHE138
CTHR184
CVAL186
CHOH414
CHOH437

Functional Information from PROSITE/UniProt
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE
ChainResidueDetails
BTYR38-GLU47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07901","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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