1hxv Summary



The structure was published by Vogtherr, M., Jacobs, D.M., Parac, T.N., et al., Ruterjans, H., Griesinger, C., and Fiebig, K.M., in 2002 in a paper entitled "NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein." (abstract).

The structure was determined using NMR spectroscopy and deposited in 2001.

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 P47480 (TIG_MYCGE)search. The sample contained 113 residues which is < 90% of the natural sequence. Out of 113 residues 85 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 P47480 (150-250) (TIG_MYCGE)search Mycoplasma genitalium G37search < 90% 113 75%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P47480 (150 - 250) TRIGGER FACTOR Mycoplasma genitalium

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A FKBP immunophilin/proline isomerasesearch Chitinase A; domain 3search FKBP-type peptidyl-prolyl cis-trans isomerasesearch, Bacterial trigger factor protein (TF)search

Chain ID Biological process (GO)
A (P47480) protein foldingsearch

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