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1nio
From Proteopedia
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| , resolution 2.00Å | |||||||
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| Ligands: | |||||||
| Activity: | rRNA N-glycosylase, with EC number 3.2.2.22 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of beta-luffin, a ribosome inactivating protein at 2.0A resolution
Overview
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.
About this Structure
1NIO is a Single protein structure of sequence from Luffa aegyptiaca. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 30 22:30:56 2008
