5cvc | pdb_00005cvc

Structure of maize serine racemase

spinqualitylabelsall models 5cvc, resolution 2.09Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5cvc is a 3 chain structure with sequence from Zea mays. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.09Å Ligands: MG, PLP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F5CAQ9_MAIZE Publication Abstract from PubMed Serine racemase (SR) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that is responsible for D-serine biosynthesis in vivo. The first X-ray crystal structure of maize SR was determined to 2.1 A resolution and PLP binding was confirmed in solution by UV-Vis absorption spectrometry. Maize SR belongs to the type II PLP-dependent enzymes and differs from the SR of a vancomycin-resistant bacterium. The PLP is bound to each monomer by forming a Schiff base with Lys67. Structural comparison with rat and fission yeast SRs reveals a similar arrangement of active-site residues but a different orientation of the C-terminal helix. Crystal structure of maize serine racemase with pyridoxal 5'-phosphate.,Zou L, Song Y, Wang C, Sun J, Wang L, Cheng B, Fan J Acta Crystallogr F Struct Biol Commun. 2016 Mar 1;72(Pt 3):165-71. doi:, 10.1107/S2053230X16000960. Epub 2016 Feb 16. PMID:26919519 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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