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Structure paper

TitleRole of phosphate chain mobility of MgATP in completing the 3-phosphoglycerate kinase catalytic site: binding, kinetic, and crystallographic studies with ATP and MgATP.
Journal, issue, pagesBiochemistry, Vol. 43, Page 3436-3449, Year 2004
Publish dateFeb 3, 2004 (structure data deposition date)
AuthorsFlachner, B. / Varga, A. / Gugolya, Z. / Vonderviszt, F. / Vas, M.
External linksBiochemistry / PubMed:15035615
MethodsX-ray diffraction
Resolution1.9 - 2.1 Å
Structure data

PDB-1vjc:
Structure of pig muscle PGK complexed with MgATP
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-1vjd:
Structure of pig muscle PGK complexed with ATP
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

Source
  • sus scrofa (pig)
KeywordsTRANSFERASE / ATP / Mg

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