3zge Summary


Greater efficiency of photosynthetic carbon fixation due to single amino acid substitution

The structure was published by Paulus, J.K., Schlieper, D., and Groth, G., in 2013 in a paper entitled "Greater Efficiency of Photosynthetic Carbon Fixation due to Single Amino Acid Substitution" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.49 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 C4 PHOSPHOENOLPYRUVATE CARBOXYLASE.

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):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A C4 PHOSPHOENOLPYRUVATE CARBOXYLASE P30694 (1-966) (CAPPA_FLATR)search Flaveria trinerviasearch 100% 990 92%
B C4 PHOSPHOENOLPYRUVATE CARBOXYLASE P30694 (1-966) (CAPPA_FLATR)search Flaveria trinerviasearch 100% 990 92%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P30694 (1 - 966) C4 PHOSPHOENOLPYRUVATE CARBOXYLASE Flaveria trinervia

Chain Sequence family (Pfam)
A, B (P30694) PF00311: Phosphoenolpyruvate carboxylasesearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A, B (P30694) carbon fixationsearch metabolic processsearch tricarboxylic acid cyclesearch C4 photosynthesissearch photosynthesissearch phosphoenolpyruvate carboxylase activitysearch catalytic activitysearch lyase activitysearch cytoplasmsearch

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