3PGM

THE STRUCTURE OF YEAST PHOSPHOGLYCERATE MUTASE AT 0.28 NM RESOLUTION

「1PGM」から置き換えられました

3PGM の概要

• エントリーDOI: 10.2210/pdb3pgm/pdb
• 分子名称: Phosphoglycerate mutase 1, SULFATE ION, 3-PHOSPHOGLYCERIC ACID (3 entities in total)
• 機能のキーワード: transferase (phosphoryl)
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm : P00950
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55094.28

構造登録者

Campbell, J.W.,Hodgson, G.I.,Warwicker, J.,Winn, S.I.,Watson, H.C. (登録日: 1982-04-06, 公開日: 1982-05-26, 最終更新日: 2024-05-22)

主引用文献

Winn, S.I.,Watson, H.C.,Harkins, R.N.,Fothergill, L.A.
Structure and activity of phosphoglycerate mutase.
Philos.Trans.R.Soc.London,Ser.B, 293:121-130, 1981

PubMed Abstract: The structure of yeast phosphoglycerate mutase determined by X-ray crystallographic and amino acid sequence studies has been interpreted in terms of the chemical, kinetic and mechanistic observations made on this enzyme. There are two histidine residues at the active site, with imidazole groups almost parallel to each other and approximately 0.4 nm apart, positioned close to the 2 and 3 positions of the substrate. The simplest interpretation of the available information suggests that a ping-pong type mechanism operates in which at least one of these histidine residues participates in the phosphoryl transfer reaction. The flexible C-terminal region also plays an important role in the enzymic reaction.

PubMed: 6115412

実験手法

X-RAY DIFFRACTION (2.8 Å)