1EDQ

CRYSTAL STRUCTURE OF CHITINASE A FROM S. MARCESCENS AT 1.55 ANGSTROMS

1EDQ の概要

• エントリーDOI: 10.2210/pdb1edq/pdb
• 関連するPDBエントリー: 1CTN
• 分子名称: CHITINASE A (2 entities in total)
• 機能のキーワード: beta-alpha (tim) barrel, hydrolase
• 由来する生物種: Serratia marcescens
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 58639.59

構造登録者

Papanikolau, Y.,Petratos, K. (登録日: 2000-01-28, 公開日: 2000-02-18, 最終更新日: 2024-10-16)

主引用文献

Papanikolau, Y.,Tavlas, G.,Vorgias, C.E.,Petratos, K.
De novo purification scheme and crystallization conditions yield high-resolution structures of chitinase A and its complex with the inhibitor allosamidin.
Acta Crystallogr.,Sect.D, 59:400-403, 2003

PubMed Abstract: The purification scheme of chitinase A (ChiA) from S. marcescens has been extensively revised. The pure enzyme crystallizes readily under new crystallization conditions. The ChiA crystal structure has been refined to 1.55 A resolution and the crystal structure of ChiA co-crystallized with the inhibitor allosamidin has been refined to 1.9 A resolution. Allosamidin is located in the deep active-site tunnel of ChiA and interacts with three important residues: Glu315, the proton donor of the catalysis, Asp313, which adopts two conformations in the native structure but is oriented towards Glu315 in the inhibitor complex, and Tyr390, which lies opposite Glu315 in the active-site tunnel.

PubMed: 12554965
DOI: 10.1107/S0907444902021923

実験手法

X-RAY DIFFRACTION (1.55 Å)