4IL5

Crystal structure of O-Acetyl Serine Sulfhydrylase from Entamoeba histolytica in complex with isoleucine

4IL5 の概要

• エントリーDOI: 10.2210/pdb4il5/pdb
• 関連するPDBエントリー: 2PQM 3BM5 4JBL 4JBN
• 分子名称: Cysteine synthase, ISOLEUCINE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: o-acetyl serine sulfhydrylase, cysteine synthase, fold type ii plp dependent enzyme, lyase, serine acetyl transferase, transferase
• 由来する生物種: Entamoeba histolytica
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74224.46

構造登録者

Raj, I.,Gourinath, S. (登録日: 2012-12-29, 公開日: 2013-12-04, 最終更新日: 2024-03-20)

主引用文献

Raj, I.,Mazumder, M.,Gourinath, S.
Molecular basis of ligand recognition by OASS from E. histolytica: insights from structural and molecular dynamics simulation studies
Biochim.Biophys.Acta, 1830:4573-4583, 2013

PubMed Abstract: O-acetyl serine sulfhydrylase (OASS) is a pyridoxal phosphate (PLP) dependent enzyme catalyzing the last step of the cysteine biosynthetic pathway. Here we analyze and investigate the factors responsible for recognition and different conformational changes accompanying the binding of various ligands to OASS.

PubMed: 23747298
DOI: 10.1016/j.bbagen.2013.05.041

実験手法

X-RAY DIFFRACTION (2.03 Å)