2qty | pdb_00002qty

Crystal Structure of mouse ADP-ribosylhydrolase 3 (mARH3)

spinqualitylabelsall models 2qty, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2qty 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. Ligands: MG Activity: Poly(ADP-ribose) glycohydrolase, with EC number 3.2.1.143 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed ADP-ribosylation is a reversible and covalent post-translational modification in which the attachment of ADP-ribose is catalyzed by ADP-ribosyltransferases and the removal of ADP-ribose is catalyzed by ADP-ribosylhydrolases. ADP-ribosylhydrolase 3 from mouse, consisting of 347 amino-acid residues, has been cloned, purified and crystallized. The three-dimensional structure has been resolved at a resolution of 1.8 A. The structure constitutes a compact all-alpha-helical protein with two Mg(2+) ions located in the active-site crevice. A structural comparison of mouse ADP-ribosylhydrolase 3 with its human orthologue shows a high degree of structural similarity. Furthermore, four prokaryotic proteins deposited in the PDB could be identified as being structurally related. Structure of mouse ADP-ribosylhydrolase 3 (mARH3).,Mueller-Dieckmann C, Kernstock S, Mueller-Dieckmann J, Weiss MS, Koch-Nolte F Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Mar 1;64(Pt, 3):156-62. Epub 2008 Feb 23. PMID:18323597 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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