2w4e

Structure of an N-terminally truncated Nudix hydrolase DR2204 from Deinococcus radiodurans

spinqualitylabelsall models 2w4e, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2w4e is a 2 chain structure with sequence from Deinococcus radiodurans R1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9RSC1_DEIRA 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 Nudix pyrophosphatases are a well represented protein family in the Deinococcus radiodurans genome. These hydrolases, which are known to be enzymatically active towards nucleoside diphosphate derivatives, play a role in cleansing the cell pool of potentially deleterious damage products. Here, the structure of DR2204, the only ADP-ribose pyrophosphatase in the D. radiodurans genome that is known to be active towards flavin adenosine dinucleotide (FAD), is presented at 2.0 angstrom resolution. Structure of an N-terminally truncated Nudix hydrolase DR2204 from Deinococcus radiodurans.,Goncalves AM, Fioravanti E, Stelter M, McSweeney S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 1;65(Pt, 11):1083-7. Epub 2009 Oct 13. PMID:19923723 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ADP-ribose pyrophosphatase 3D structures Nudix hydrolase 3D structures

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