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Structure paper

TitleStructural basis for allosteric regulation of pyruvate kinase M2 by phosphorylation and acetylation.
Journal, issue, pagesJ. Biol. Chem., Vol. 295, Page 17425-17440, Year 2020
Publish dateApr 26, 2020 (structure data deposition date)
AuthorsNandi, S. / Razzaghi, M. / Srivastava, D. / Dey, M.
External linksJ. Biol. Chem. / PubMed:33453989
MethodsX-ray diffraction
Resolution1.84 - 2.45 Å
Structure data

PDB-6wp3:
Pyruvate Kinase M2 Mutant-K433Q
Method: X-RAY DIFFRACTION / Resolution: 1.84 Å

PDB-6wp4:
Pyruvate Kinase M2 mutant-S37E
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-6wp5:
Pyruvate Kinase M2 mutant-S37D
Method: X-RAY DIFFRACTION / Resolution: 2.17 Å

PDB-6wp6:
Pyruvate Kinase M2 mutant-S37E K433E
Method: X-RAY DIFFRACTION / Resolution: 2.45 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-OXL:
OXALATE ION

ChemComp-MG:
Unknown entry

ChemComp-NO3:
NITRATE ION

ChemComp-K:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

ChemComp-FBP:
1,6-di-O-phosphono-beta-D-fructofuranose

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / GLYCOLYSIS / GENE REGULATION / PHOSPHOTRANSFERASE

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