1jqn Summary

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Crystal structure of E.coli phosphoenolpyruvate carboxylase in complex with Mn2+ and DCDP

The structure was published by Matsumura, H., Xie, Y., Shirakata, S., et al., Ueno, Y., Izui, K., and Kai, Y., in 2002 in a paper entitled "Crystal structures of C4 form maize and quaternary complex of E. coli phosphoenolpyruvate carboxylases." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.35 Å and deposited in 2001.

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)search. 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 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):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A phosphoenolpyruvate carboxylase P00864 (1-883) (CAPP_ECOLI)search Escherichia coli K-12search 100% 883 98%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00864 (1 - 883) phosphoenolpyruvate carboxylase Escherichia coli

Chain Structural classification (SCOP) Sequence family (Pfam)
A (P00864) Phosphoenolpyruvate carboxylasesearch PF00311: Phosphoenolpyruvate carboxylasesearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P00864) magnesium ion bindingsearch catalytic activitysearch phosphoenolpyruvate carboxylase activitysearch lyase activitysearch cytosolsearch tricarboxylic acid cyclesearch oxaloacetate metabolic processsearch metabolic processsearch carbon fixationsearch

Chain InterPro annotation
A Pyruvate/Phosphoenolpyruvate kinase-like domainsearch Phosphoenolpyruvate carboxylase, active sitesearch Phosphoenolpyruvate carboxylasesearch Phosphoenolpyruvate carboxylase, bacterial/plant-typesearch