3e2f

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Crystal structure of mouse kynurenine aminotransferase III, PLP-bound formCrystal structure of mouse kynurenine aminotransferase III, PLP-bound form

Structural highlights

3e2f is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.59Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KAT3_MOUSE Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). May catalyze the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (By similarity). Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2-oxoglutarate as amino group acceptor (in vitro).[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. Han Q, Robinson H, Cai T, Tagle DA, Li J. Biochemical and structural properties of mouse kynurenine aminotransferase III. Mol Cell Biol. 2009 Feb;29(3):784-93. Epub 2008 Nov 24. PMID:19029248 doi:http://dx.doi.org/10.1128/MCB.01272-08

3e2f, resolution 2.59Å

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OCA