2uz5 Summary

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SOLUTION STRUCTURE OF THE FKBP-DOMAIN OF LEGIONELLA PNEUMOPHILA MIP

The structure was published by Horstmann, M., Ehses, P., Schweimer, K., et al., Hacker, J., Rosch, P., and Faber, C., in 2006 in a paper entitled "Domain Motions of the Mip Protein from Legionella Pneumophila" (abstract).

The structure was determined using NMR spectroscopy and deposited in 2007.

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

The PDB entry contains the structure of MACROPHAGE INFECTIVITY POTENTIATOR. This molecule has the UniProt identifier Q5ZXE0 (MIP_LEGPH)search. The sample contained 137 residues which is < 90% of the natural sequence. Out of 137 residues 137 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 MACROPHAGE INFECTIVITY POTENTIATOR Q5ZXE0 (97-233) (MIP_LEGPH)search Legionella pneumophila subsp. pneumophila str. Philadelphia 1search 100% 137 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q5ZXE0 (97 - 233) MACROPHAGE INFECTIVITY POTENTIATOR Legionella pneumophila

Chain Sequence family (Pfam)
A (Q5ZXE0) PF00254: FKBP-type peptidyl-prolyl cis-trans isomerasesearch, PF01346: Domain amino terminal to FKBP-type peptidyl-prolyl isomerasesearch

Chain ID Biological process (GO)
A (Q5ZXE0) protein foldingsearch

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