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5OWJ

The dynamic dimer structure of the chaperone Trigger Factor (conformer 2)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006457biological_processprotein folding
A0009408biological_processresponse to heat
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0042802molecular_functionidentical protein binding
A0043022molecular_functionribosome binding
A0043335biological_processprotein unfolding
A0044183molecular_functionprotein folding chaperone
A0051083biological_process'de novo' cotranslational protein folding
A0051301biological_processcell division
A0061077biological_processchaperone-mediated protein folding
A1990169biological_processstress response to copper ion
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006457biological_processprotein folding
B0009408biological_processresponse to heat
B0015031biological_processprotein transport
B0016020cellular_componentmembrane
B0042802molecular_functionidentical protein binding
B0043022molecular_functionribosome binding
B0043335biological_processprotein unfolding
B0044183molecular_functionprotein folding chaperone
B0051083biological_process'de novo' cotranslational protein folding
B0051301biological_processcell division
B0061077biological_processchaperone-mediated protein folding
B1990169biological_processstress response to copper ion
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: ADP-ribosylarginine => ECO:0000269|PubMed:16112649
ChainResidueDetails
AARG45
BARG45

221716

PDB entries from 2024-06-26

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