Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase with surface mutation D44G from Burkholderia pseudomallei complexed with CJ168
The structure was published by Begley, D.W., Fox, D., Jenner, D., et al., Sarkar-Tyson, M., Edwards, T.E., and Lorimer, D.D., in 2014 in a paper entitled "A structural biology approach enables the development of antimicrobials targeting bacterial immunophilins." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.75 Å and deposited in 2012.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of Ubiquitin-like protein SMT3, Peptidyl-prolyl cis-trans isomerase.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.
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):