1EPQ

ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN) COMPLEXED WITH PD-133,450 (SOT PHE GLY+SCC GCL)

1EPQ の概要

• エントリーDOI: 10.2210/pdb1epq/pdb
• 関連するPDBエントリー: 1epp
• 関連するBIRD辞書のPRD_ID: PRD_000356
• 分子名称: ENDOTHIAPEPSIN, N-[(1S)-2-{[(2S,3R,4S)-1-cyclohexyl-3,4-dihydroxy-6-methylheptan-2-yl]amino}-1-(ethylsulfanyl)-2-oxoethyl]-Nalpha-(morp holin-4-ylsulfonyl)-L-phenylalaninamide, SULFATE ION, ... (4 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 (chestnut blight fungus)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34662.88

構造登録者

Dealwis, C.,Cooper, J.B.,Blundell, T.L. (登録日: 1994-07-27, 公開日: 1994-12-20, 最終更新日: 2024-10-23)

主引用文献

Lunney, E.A.,Hamilton, H.W.,Hodges, J.C.,Kaltenbronn, J.S.,Repine, J.T.,Badasso, M.,Cooper, J.B.,Dealwis, C.,Wallace, B.A.,Lowther, W.T.
Analyses of ligand binding in five endothiapepsin crystal complexes and their use in the design and evaluation of novel renin inhibitors.
J.Med.Chem., 36:3809-3820, 1993

PubMed Abstract: Five renin inhibitors were cocrystallized with endothiapepsin, a fungal enzyme homologous to renin. Crystal structures of inhibitor-bound complexes have provided invaluable insight regarding the three-dimensional structure of the aspartic proteinase family of enzymes, as well as the steric and polar interactions that occur between the proteins and the bound ligands. Beyond this, subtleties of binding have been revealed, including multiple subsite binding modes and subsite interdependencies. This information has been applied in the design of novel potent renin inhibitors and in the understanding of structure-activity relationships and enzyme selectivities.

PubMed: 8254610
DOI: 10.1021/jm00076a008

実験手法

X-RAY DIFFRACTION (1.9 Å)