4LP9

Endothiapepsin complexed with Phe-reduced-Tyr peptide.

4LP9 の概要

• エントリーDOI: 10.2210/pdb4lp9/pdb
• 関連するPDBエントリー: 1GVT 1GVU 1GVV 1GVW 1GVX
• 関連するBIRD辞書のPRD_ID: PRD_001157
• 分子名称: Endothiapepsin, Ser-Leu-Phe-His-Phenylalanyl-reduced-peptide-bond-Tyrosyl-Thr-Pro, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: aspartic proteinase fold, proteolysis, hydrolase (acid proteinase), hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Cryphonectria parasitica (Chesnut blight fungus)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35652.76

構造登録者

Guo, J.,Cooper, J.B.,Wood, S.P. (登録日: 2013-07-15, 公開日: 2014-01-15, 最終更新日: 2024-11-20)

主引用文献

Guo, J.,Cooper, J.B.,Wood, S.P.
The structure of endothiapepsin complexed with a Phe-Tyr reduced-bond inhibitor at 1.35 angstrom resolution.
Acta Crystallogr F Struct Biol Commun, 70:30-33, 2014

PubMed Abstract: Endothiapepsin is a typical member of the aspartic proteinase family. The catalytic mechanism of this family is attributed to two conserved catalytic aspartate residues, which coordinate the hydrolysis of a peptide bond. An oligopeptide inhibitor (IC50 = 0.62 µM) based on a reduced-bond transition-state inhibitor of mucorpepsin was co-crystallized with endothiapepsin and the crystal structure of the enzyme-inhibitor complex was determined at 1.35 Å resolution. A total of 12 hydrogen bonds between the inhibitor and the active-site residues were identified. The resulting structure demonstrates a number of novel subsite interactions in the active-site cleft.

PubMed: 24419612
DOI: 10.1107/S2053230X13032974

実験手法

X-RAY DIFFRACTION (1.35 Å)