2BAX

Atomic Resolution Structure of the Double Mutant (K53,56M) of Bovine Pancreatic Phospholipase A2

2BAX の概要

• エントリーDOI: 10.2210/pdb2bax/pdb
• 関連するPDBエントリー: 1MKT 1UNE 1VL9
• 分子名称: Phospholipase A2, CALCIUM ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: phospholipase a2, alpha helix, beta sheet, hydrolase
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Secreted: P00593
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14480.94

構造登録者

Sekar, K.,Yogavel, M.,Velmurugan, D.,Dauter, Z.,Dauter, M.,Tsai, M.D. (登録日: 2005-10-15, 公開日: 2005-10-25, 最終更新日: 2024-10-30)

主引用文献

Sekar, K.,Rajakannan, V.,Gayathri, D.,Velmurugan, D.,Poi, M.J.,Dauter, M.,Dauter, Z.,Tsai, M.D.
Atomic resolution (0.97 A) structure of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2.
Acta Crystallogr.,Sect.F, 61:3-7, 2005

PubMed Abstract: The enzyme phospholipase A2 catalyzes the hydrolysis of the sn-2 acyl chain of phospholipids, forming fatty acids and lysophospholipids. The crystal structure of a triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2 in which the lysine residues at positions 53, 56 and 121 are replaced recombinantly by methionines has been determined at atomic resolution (0.97 A). The crystal is monoclinic (space group P2), with unit-cell parameters a = 36.934, b = 23.863, c = 65.931 A, beta = 101.47 degrees. The structure was solved by molecular replacement and has been refined to a final R factor of 10.6% (Rfree = 13.4%) using 63,926 unique reflections. The final protein model consists of 123 amino-acid residues, two calcium ions, one chloride ion, 243 water molecules and six 2-methyl-2,4-pentanediol molecules. The surface-loop residues 60-70 are ordered and have clear electron density.

PubMed: 16508077
DOI: 10.1107/S1744309104021748

実験手法

X-RAY DIFFRACTION (1.1 Å)