1nio | pdb_00001nio
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Crystal structure of beta-luffin, a ribosome inactivating protein at 2.0A resolution
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Structural highlights
FunctionEvolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References | ||||||||||||||||||||
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