2W4E
Structure of an N-terminally truncated Nudix hydrolase DR2204 from Deinococcus radiodurans
Summary for 2W4E
| Entry DOI | 10.2210/pdb2w4e/pdb |
| Descriptor | MUTT/NUDIX FAMILY PROTEIN (2 entities in total) |
| Functional Keywords | adp-ribose pyrophosphatase, hydrolase |
| Biological source | DEINOCOCCUS RADIODURANS |
| Total number of polymer chains | 2 |
| Total formula weight | 31213.73 |
| Authors | Goncalves, A.M.D.,Fioravanti, E.,Stelter, M.,McSweeney, S. (deposition date: 2008-11-25, release date: 2009-12-01, Last modification date: 2024-05-08) |
| Primary citation | Goncalves, A.M.D.,Fioravanti, E.,Stelter, M.,Mcsweeney, S. Structure of an N-Terminally Truncated Nudix Hydrolase Dr2204 from Deinococcus Radiodurans. Acta Crystallogr.,Sect.F, 65:1083-, 2009 Cited by PubMed Abstract: 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. PubMed: 19923723DOI: 10.1107/S1744309109037191 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report
