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Structure paper

Title3D structural analysis of protein O-mannosyl kinase, POMK, a causative gene product of dystroglycanopathy.
Journal, issue, pagesGenes Cells, Vol. 22, Page 348-359, Year 2017
Publish dateSep 27, 2016 (structure data deposition date)
AuthorsNagae, M. / Mishra, S.K. / Neyazaki, M. / Oi, R. / Ikeda, A. / Matsugaki, N. / Akashi, S. / Manya, H. / Mizuno, M. / Yagi, H. ...Nagae, M. / Mishra, S.K. / Neyazaki, M. / Oi, R. / Ikeda, A. / Matsugaki, N. / Akashi, S. / Manya, H. / Mizuno, M. / Yagi, H. / Kato, K. / Senda, T. / Endo, T. / Nogi, T. / Yamaguchi, Y.
External linksGenes Cells / PubMed:28251761
MethodsX-ray diffraction
Resolution2.4 - 2.5 Å
Structure data

PDB-5gz8:
Crystal structure of catalytic domain of Protein O-mannosyl Kinase in ligand-free form
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-5gz9:
Crystal structure of catalytic domain of Protein O-mannosyl Kinase in complexes with AMP-PNP, Magnesium ions and glycopeptide
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-MAN:
alpha-D-mannopyranose

Source
  • mus musculus (house mouse)
KeywordsTRANSFERASE / Sugar Kinase / Dystroglycanopathy / O-mannosylation

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