2yep | pdb_00002yep

STRUCTURE OF AN N-TERMINAL NUCLEOPHILE (NTN) HYDROLASE, OAT2, IN COMPLEX WITH GLUTAMATE

spinqualitylabelsall models 2yep, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2yep is a 8 chain structure with sequence from Streptomyces clavuligerus. This structure supersedes the now removed PDB entry 2w4n. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: ACT, GLU, TH5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GNAT2_STRCL Catalyzes the biosynthesis of ornithine by transacetylation between N(2)-acetylornithine and glutamate. It can also use L-arginine, L-glutamine and L-lysine as acetyl acceptors. Publication Abstract from PubMed Structural and biochemical analyses reveal how ornithine acetyl-transferases catalyse the reversible transfer of an acetyl-group from a basic (ornithine) to an acidic (glutamate) amino acid by employing a common mechanism involving an acetyl-enzyme intermediate but using different side chain binding modes. Structural and biochemical analyses reveal how ornithine acetyl transferase binds acidic and basic amino acid substrates.,Iqbal A, Clifton IJ, Chowdhury R, Ivison D, Domene C, Schofield CJ Org Biomol Chem. 2011 Sep 21;9(18):6219-25. Epub 2011 Jul 28. PMID:21796301 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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