Selective targeting of disease-relevant protein binding domains by O-phosphorylated natural product derivatives
The structure was published by Graber, M., Janczyk, W., Sperl, B., et al., Hausch, F., Holak, T.A., and Berg, T., in 2011 in a paper entitled "Selective targeting of disease-relevant protein binding domains by o-phosphorylated natural product derivatives." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.4 Å and deposited in 2011.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1. This molecule has the UniProt identifier Q13526 (PIN1_HUMAN). The sample contained 166 residues which is 100% of the natural sequence. Out of 166 residues 142 were observed and are deposited in the PDB.
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 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):
This entry contains 1 unique UniProt protein: