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TitleKinetic and mutational studies of the adenosine diphosphate ribose hydrolase from Mycobacterium tuberculosis.
Journal, issue, pagesJ. Bioenerg. Biomembr., Vol. 48, Page 557-567, Year 2016
Publish dateFeb 19, 2016 (structure data deposition date)
AuthorsO'Handley, S.F. / Thirawatananond, P. / Kang, L.W. / Cunningham, J.E. / Leyva, J.A. / Amzel, L.M. / Gabelli, S.B.
External linksJ. Bioenerg. Biomembr. / PubMed:27683242
MethodsX-ray diffraction
Resolution2 Å
Structure data

PDB-5i8u:
Crystal Structure of the RV1700 (MT ADPRASE) E142Q mutant
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-FMT:
FORMIC ACID

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsHYDROLASE / NUDIX / nudix hydrolase / ADP-ribose hydrolase / ADPRase / ADPr hydrolase

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