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2IOQ

Crystal Structure of full-length HTPG, the Escherichia coli HSP90

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006457biological_processprotein folding
A0006974biological_processDNA damage response
A0009408biological_processresponse to heat
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043093biological_processFtsZ-dependent cytokinesis
A0044183molecular_functionprotein folding chaperone
A0048471cellular_componentperinuclear region of cytoplasm
A0051082molecular_functionunfolded protein binding
A0051087molecular_functionprotein-folding chaperone binding
A0140662molecular_functionATP-dependent protein folding chaperone
B0000166molecular_functionnucleotide binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006457biological_processprotein folding
B0006974biological_processDNA damage response
B0009408biological_processresponse to heat
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0043093biological_processFtsZ-dependent cytokinesis
B0044183molecular_functionprotein folding chaperone
B0048471cellular_componentperinuclear region of cytoplasm
B0051082molecular_functionunfolded protein binding
B0051087molecular_functionprotein-folding chaperone binding
B0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PROSITE/UniProt
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE
ChainResidueDetails
ATYR25-GLU34

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:15837196
ChainResidueDetails
AASN38
BHIS255
AASP80
APHE127
ATHR174
AHIS255
BASN38
BASP80
BPHE127
BTHR174

218853

PDB entries from 2024-04-24

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