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Nudix hydrolase

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<StructureSection load='1su2' size='450' side='right' caption='Structure of Nudix hydrolase MutT complex with ATP and Mg+2 ion (green) (PDB entry [[1su2]])' scene='48/488532/Cv/1'>
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<StructureSection load='1su2' size='400' side='right' caption='Structure of Nudix hydrolase MutT complex with ATP and Mg+2 ion (green) (PDB entry [[1su2]])' scene='48/488532/Cv/1'>
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== Function ==
== Function ==

Revision as of 12:55, 24 July 2019

Structure of Nudix hydrolase MutT complex with ATP and Mg+2 ion (green) (PDB entry 1su2)

Drag the structure with the mouse to rotate

3D structures of Nudix hydrolase

Updated on 24-July-2019


2b0v, 3cng - NDX - Nitrosomonas europaea
1k2e, 1jrk, 1k26 - NDX (mutant) - Pyrobaculum aerophilum
1sjy, 1soi, 2w4e - DrNDX - Deinococcus radiodurans
1su2 - DrNDX + ATP
1sz3 - DrNDX + GNP
3fcm, 3f6a - NDX - Clostridium perfringens
3qsj - NDX - Alicyclobacillus acidocaldarius
3r03 - NDX - Rhodospirillum rubrum
2azw, 2fml - NDX - Enterococcus faecalis
2b06, 2pqv - NDX - Streptococcus pneumoniae
3exq - NDX - Lactobacillus brevis
3i9x - NDX - Listeria innocua
3id9, 3smd - NDX - Bacillus thuringiensis
4dyw - NDX - Burkholderia pseudomallei

References

  1. ↑ McLennan AG. The Nudix hydrolase superfamily. Cell Mol Life Sci. 2006 Jan;63(2):123-43. doi: 10.1007/s00018-005-5386-7. PMID:16378245 doi:http://dx.doi.org/10.1007/s00018-005-5386-7
  2. ↑ Sheikh S, O'Handley SF, Dunn CA, Bessman MJ. Identification and characterization of the Nudix hydrolase from the Archaeon, Methanococcus jannaschii, as a highly specific ADP-ribose pyrophosphatase. J Biol Chem. 1998 Aug 14;273(33):20924-8. PMID:9694840
  3. ↑ McLennan AG. The MutT motif family of nucleotide phosphohydrolases in man and human pathogens (review). Int J Mol Med. 1999 Jul;4(1):79-89. PMID:10373642
  4. ↑ Ranatunga W, Hill EE, Mooster JL, Holbrook EL, Schulze-Gahmen U, Xu W, Bessman MJ, Brenner SE, Holbrook SR. Structural studies of the Nudix hydrolase DR1025 from Deinococcus radiodurans and its ligand complexes. J Mol Biol. 2004 May 21;339(1):103-16. PMID:15123424 doi:http://dx.doi.org/10.1016/j.jmb.2004.01.065

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