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Structure paper

TitleTyr26 phosphorylation of PGAM1 provides a metabolic advantage to tumours by stabilizing the active conformation.
Journal, issue, pagesNat Commun, Vol. 4, Page 1790-1790, Year 2013
Publish dateAug 21, 2012 (structure data deposition date)
AuthorsHitosugi, T. / Zhou, L. / Fan, J. / Elf, S. / Zhang, L. / Xie, J. / Wang, Y. / Gu, T.L. / Aleckovic, M. / Leroy, G. ...Hitosugi, T. / Zhou, L. / Fan, J. / Elf, S. / Zhang, L. / Xie, J. / Wang, Y. / Gu, T.L. / Aleckovic, M. / Leroy, G. / Kang, Y. / Kang, H.B. / Seo, J.H. / Shan, C. / Jin, P. / Gong, W. / Lonial, S. / Arellano, M.L. / Khoury, H.J. / Chen, G.Z. / Shin, D.M. / Khuri, F.R. / Boggon, T.J. / Kang, S. / He, C. / Chen, J.
External linksNat Commun / PubMed:23653202
MethodsX-ray diffraction
Resolution1.65 - 2.0817 Å
Structure data

PDB-4gpi:
Crystal structure of human B type phosphoglycerate mutase
Method: X-RAY DIFFRACTION / Resolution: 2.0817 Å

PDB-4gpz:
Crystal structure of human B type phosphoglycerate mutase H11 phosphorylated form
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

Source
  • homo sapiens (human)
KeywordsIsomerase / hydrolase / alpha/beta

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