2ER6

The structure of a synthetic pepsin inhibitor complexed with endothiapepsin.

2ER6 の概要

• エントリーDOI: 10.2210/pdb2er6/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000346
• 分子名称: ENDOTHIAPEPSIN, H-256 peptide (3 entities in total)
• 機能のキーワード: hydrolase-hydrolase inhibitor complex, acid proteinase, hydrolase/hydrolase inhibitor
• 由来する生物種: Cryphonectria parasitica
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34725.87

構造登録者

Cooper, J.B.,Foundling, S.I.,Szelke, M.,Blundell, T.L. (登録日: 1990-10-13, 公開日: 1991-01-15, 最終更新日: 2024-11-20)

主引用文献

Cooper, J.,Foundling, S.,Hemmings, A.,Blundell, T.,Jones, D.M.,Hallett, A.,Szelke, M.
The structure of a synthetic pepsin inhibitor complexed with endothiapepsin
Eur.J.Biochem., 169:215-221, 1987

PubMed Abstract: The conformation of a synthetic polypeptide inhibitor, bound to the active site of the fungal aspartic proteinase endothiapepsin (EC 3.4.23.6), has been determined by X-ray diffraction at 0.20-nm resolution and refined to an agreement factor of 0.20. The inhibitor: Pro Thr Glu Phe-R-Phe Arg Glu (R = -CH2NH-) is based on a chromogenic substrate of pepsin (EC 3.4.23.1). It has, in place of the scissile bond, a reduced peptide group which is resistant to hydrolysis and mimics the tetrahedral transition state. The inhibitor binds in an extended conformation with the reduced bond close to the essential aspartate side-chains of the enzyme. The hydrogen bonds and hydrophobic interactions between the enzyme and the inhibitor do not induce large conformational changes.

PubMed: 3119339
DOI: 10.1111/j.1432-1033.1987.tb13600.x

実験手法

X-RAY DIFFRACTION (2 Å)