CRYSTAL STRUCTURE OF MN(2+)-BOUND PHOSPHOENOLPYRUVATE CARBOXYLASE
The structure was published by Matsumura, H., Terada, M., Shirakata, S., et al., Yoshinaga, T., Izui, K., and Kai, Y., in 1999 in a paper entitled "Plausible phosphoenolpyruvate binding site revealed by 2.6 A structure of Mn2+-bound phosphoenolpyruvate carboxylase from Escherichia coli" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.6 Å and deposited in 1999.
The experimental data on which the structure is based was also 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 867 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 most likely forms homotetramers.
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: