3prd Summary

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Structural analysis of protein folding by the Methanococcus jannaschii chaperone FKBP26

The structure was published by Martinez-Hackert, E. and Hendrickson, W.A., in 2011 in a paper entitled "Structural Analysis of Protein Folding by the Long-Chain Archaeal Chaperone FKBP26." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.3 Å and deposited in 2010.

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

The PDB entry contains the structure of FKBP-type peptidyl-prolyl cis-trans isomerase. This molecule has the UniProt identifier Q58235 (FKBP2_METJA)search. The sample contained 231 residues which is 100% of the natural sequence. Out of 231 residues 222 were observed and are deposited in the PDB.

The molecule most likely forms homodimers.

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 FKBP-type peptidyl-prolyl cis-trans isomerase Q58235 (1-231) (FKBP2_METJA)search Methanocaldococcus jannaschii DSM 2661search 100% 231 96%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q58235 (1 - 231) FKBP-type peptidyl-prolyl cis-trans isomerase Methanocaldococcus jannaschii

Chain Sequence family (Pfam)
A (Q58235) PF00254: FKBP-type peptidyl-prolyl cis-trans isomerasesearch

Chain ID Molecular function (GO) Biological process (GO)
A (Q58235) peptidyl-prolyl cis-trans isomerase activitysearch isomerase activitysearch protein peptidyl-prolyl isomerizationsearch protein foldingsearch

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