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Structure paper

TitleDivalent metal ion-based catalytic mechanism of the Nudix hydrolase Orf153 (YmfB) from Escherichia coli
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 70, Page 1297-1310, Year 2014
Publish dateNov 1, 2013 (structure data deposition date)
AuthorsHong, M.K. / Ribeiro, A.J.M. / Kim, J.K. / Ngo, H.P.T. / Kim, J. / Lee, C.H. / Ahn, Y.J. / Fernandes, P.A. / Li, Q. / Ramos, M.J. / Kang, L.W.
External linksActa Crystallogr. ,Sect. D / PubMed:24816099
MethodsX-ray diffraction
Resolution2.3 - 2.69 Å
Structure data

PDB-4nfw:
Structure and atypical hydrolysis mechanism of the Nudix hydrolase Orf153 (YmfB) from Escherichia coli
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-4nfx:
Structure and atypical hydrolysis mechanism of the Nudix hydrolase Orf153 (YmfB) from Escherichia coli
Method: X-RAY DIFFRACTION / Resolution: 2.69 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / Nudix hydrolase; YmfB; Nucleoside triphosphatase; Metal ions-based catalysis / Nudix motif / phophatase / phosphatase

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