1nio | pdb_00001nio

Crystal structure of beta-luffin, a ribosome inactivating protein at 2.0A resolution

spinqualitylabelsall models 1nio, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1nio is a 1 chain structure with sequence from Lufae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAG Activity: rRNA N-glycosylase, with EC number 3.2.2.22 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 The crystal structure of beta-luffin at 2.0 A resolution was solved by the molecular-replacement method using polyalanyl trichosanthin as the search model. The structure was refined with CNS1.1, giving R(work) = 0.162 and R(free) = 0.204. The r.m.s.d.s of the bond lengths and bond angles are 0.008 A and 1.3 degrees, respectively. The overall structure is similar to those of other type I RIPs. Three N-acetylglucosamine (Nag) molecules are linked to residues Asn2, Asn78 and Asn85 of the protein. Crystal structure of beta-luffin, a ribosome-inactivating protein, at 2.0 A resolution.,Ma QJ, Li JH, Li HG, Wu S, Dong YC Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1366-70. Epub 2003, Jul 23. PMID:12876337 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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