1EPQ

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

Summary for 1EPQ

• Entry DOI: 10.2210/pdb1epq/pdb
• Related: 1epp
• Related PRD ID: PRD_000356
• Descriptor: 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)
• Functional Keywords: hydrolase-hydrolase inhibitor complex, acid proteinase, hydrolase/hydrolase inhibitor
• Biological source: Cryphonectria parasitica (chestnut blight fungus)
• Total number of polymer chains: 1
• Total formula weight: 34662.88

Authors

Dealwis, C.,Cooper, J.B.,Blundell, T.L. (deposition date: 1994-07-27, release date: 1994-12-20, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)