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Structure paper

TitleStructure and Function of Human Erythrocyte Pyruvate Kinase. Molecular Basis of Nonspherocytic Hemolytic Anemia.
Journal, issue, pagesJ. Biol. Chem., Vol. 277, Page 23807-, Year 2002
Publish dateNov 12, 2007 (structure data deposition date)
AuthorsValentini, G. / Chiarelli, L.R. / Fortin, R. / Dolzan, M. / Galizzi, A. / Abraham, D.J. / Wang, C. / Bianchi, P. / Zanella, A. / Mattevi, A.
External linksJ. Biol. Chem. / PubMed:11960989
MethodsX-ray diffraction
Resolution2.73 - 2.87 Å
Structure data

PDB-2vgb:
HUMAN ERYTHROCYTE PYRUVATE KINASE
Method: X-RAY DIFFRACTION / Resolution: 2.73 Å

PDB-2vgf:
HUMAN ERYTHROCYTE PYRUVATE KINASE: T384M mutant
Method: X-RAY DIFFRACTION / Resolution: 2.75 Å

PDB-2vgg:
HUMAN ERYTHROCYTE PYRUVATE KINASE: R479H MUTANT
Method: X-RAY DIFFRACTION / Resolution: 2.74 Å

PDB-2vgi:
HUMAN ERYTHROCYTE PYRUVATE KINASE: R486W MUTANT
Method: X-RAY DIFFRACTION / Resolution: 2.87 Å

Chemicals

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

ChemComp-PGA:
2-PHOSPHOGLYCOLIC ACID

ChemComp-K:
Unknown entry

ChemComp-MN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / METAL-BINDING / PHOSPHORYLATION / PYRUVATE KINASE IN THE ACTIVE R-STATE / KINASE / PYRUVATE / MAGNESIUM / GLYCOLYSIS / DISEASE MUTATION / R-STATE

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