THREE-DIMENSIONAL STRUCTURE OF PHOSPHOENOLPYRUVATE CARBOXYLASE FROM ESCHERICHIA COLI AT 2.8 A RESOLUTION
The structure was published by Kai, Y., Matsumura, H., Inoue, T., et al., Kihara, A., Tsumura, K., and Izui, K., in 1999 in a paper entitled "Three-dimensional structure of phosphoenolpyruvate carboxylase: a proposed mechanism for allosteric inhibition." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.8 Å and deposited in 1998.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of PHOSPHOENOLPYRUVATE CARBOXYLASE. This molecule has the UniProt identifier P00864 (CAPP_ECOLI). The sample contained 883 residues which is 100% of the natural sequence. Out of 883 residues 873 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 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):
This entry contains 1 unique UniProt protein: