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Crystal structure of E. coli glyoxylate carboligase

The structure was published by Kaplun, A., Binshtein, E., Vyazmensky, M., et al., Chipman, D.M., Tittmann, K., and Shaanan, B., in 2008 in a paper entitled "Glyoxylate carboligase lacks the canonical active site glutamate of thiamine-dependent enzymes." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.7 Å and deposited in 2007.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of Glyoxylate carboligase.

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 Glyoxylate carboligase P0AEP7 (1-593) (GCL_ECOLI)search Escherichia coli K-12search 100% 616 96%
B Glyoxylate carboligase P0AEP7 (1-593) (GCL_ECOLI)search Escherichia coli K-12search 100% 616 96%
C Glyoxylate carboligase P0AEP7 (1-593) (GCL_ECOLI)search Escherichia coli K-12search 100% 616 96%
D Glyoxylate carboligase P0AEP7 (1-593) (GCL_ECOLI)search Escherichia coli K-12search 100% 616 96%
E Glyoxylate carboligase P0AEP7 (1-593) (GCL_ECOLI)search Escherichia coli K-12search 100% 616 96%
F Glyoxylate carboligase P0AEP7 (1-593) (GCL_ECOLI)search Escherichia coli K-12search 100% 616 96%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P0AEP7 (1 - 593) Glyoxylate carboligase Escherichia coli

Chain Sequence family (Pfam)
A, B, C, D, E, F (P0AEP7) PF00205: Thiamine pyrophosphate enzyme, central domainsearch, PF02775: Thiamine pyrophosphate enzyme, C-terminal TPP binding domainsearch, PF02776: Thiamine pyrophosphate enzyme, N-terminal TPP binding domainsearch

Chain ID Molecular function (GO) Biological process (GO)
A, B, C, D, E, F (P0AEP7) lyase activitysearch tartronate-semialdehyde synthase activitysearch thiamine pyrophosphate bindingsearch catalytic activitysearch magnesium ion bindingsearch glyoxylate catabolic processsearch glycolate catabolic processsearch

Chain InterPro annotation
A, B, C, D, E, F Glyoxylate carboligasesearch Thiamine pyrophosphate enzyme, C-terminal TPP-bindingsearch Thiamine pyrophosphate enzyme, central domainsearch Thiamine pyrophosphate enzyme, N-terminal TPP-binding domainsearch