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). 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):
This entry contains 1 unique UniProt protein: