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Literature summary for 2.2.1.1 extracted from

  • Obiol-Pardo, C.; Rubio-Martinez, J.
    Homology modeling of human transketolase: description of critical sites useful for drug design and study of the cofactor binding mode (2009), J. Mol. Graph. Model., 27, 723-734.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
homology modeling of human transketolase using the crystal structure of yeast as a template, refinement of the model through molecular dynamics simulations. Five critical sites containing arginines R101, R318, R395, R401 and R474 contribute to dimer stability or catalytic activity. R101 and R401 maintain hydrogen bonds within the dimer, the most important being with D424 and E432, respectively. Both bonds are formed by charged residues. Non-conserved R395 also forms stable intermolecular hydrogen bonds. There is a substrate channel similar to the yeast enzyme Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate homology modeling. The aminopyrimidine ring of thiamine diphosphate establishes weak hydrogen bonds, main interactions are focused on the diphosphate moiety, which maintains seven stable hydrogen bonds. H77, which forms a hydrogen bond with the diphosphate, is a conserved residue. Presence of a substrate channel Homo sapiens