1l1p Summary


Solution Structure of the PPIase Domain from E. coli Trigger Factor

A publication describing this structure is not available. The depositing authors are Kozlov, G.search; Trempe, J.-F.search; Perreault, A.search; Wong, M.search; Denisov, A.search; Ghandi, S.search; Gehring, K.search; Ekiel, I.search; Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI)search

The structure was determined using NMR spectroscopy and deposited in 2002.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of trigger factor. This molecule has the UniProt identifier P0A850 (TIG_ECOLI)search. The sample contained 106 residues which is < 90% of the natural sequence. Out of 106 residues 106 were observed and are deposited in the PDB.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A trigger factor P0A850 (148-249) (TIG_ECOLI)search Escherichia coli K-12search 100% 106 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P0A850 (148 - 249) trigger factor Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P0A850) FKBP immunophilin/proline isomerasesearch Chitinase A; domain 3search PF00254: FKBP-type peptidyl-prolyl cis-trans isomerasesearch

Chain ID Biological process (GO)
A (P0A850) protein foldingsearch

Chain InterPro annotation
A Peptidyl-prolyl cis-trans isomerase, FKBP-type, domainsearch