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Literature summary for 2.7.2.3 extracted from

  • Flachner, B.; Kovari, Z.; Varga, A.; Gugolya, Z.; Vonderviszt, F.; Naray-Szabo, G.; Vas, M.
    Role of phosphate chain mobility of MgATP in completing the 3-phosphoglycerate kinase catalytic site: binding, kinetic, and crystallographic studies with ATP and MgATP (2004), Biochemistry, 43, 3436-3449.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
single crystals of the binary complexes with ATP (at 1.9 A resolution) and MgATP2- (at 2.1 A resolution) are grown in hanging drops, at 15°C, within about 2 weeks Sus scrofa

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ MgATP2- is the substrate. Mg2+ is liganded to both beta- and gamma-phosphates of ATP Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Sus scrofa
-

Synonyms

Synonyms Comment Organism
PGK
-
Sus scrofa