DHI-PRO-PHE-HIS-LEU-LEU-VAL-TYR (chain I)
PRO-HIS-PRO-PHE-HIS-LAV-ILE-HIS-LYS (chain I)
THR-PHE-GLN-ALA-PSA-LEU-ARG-GLU (chain I)
BOC-HIS-PRO-PHE-HIS-LOV-ILE-HIS (chain B)
BOC-HIS-PRO-PHE-ALA-LOV-ILE-HIS (chain B)
IVA-HIS-PRO-PHE-HIS-CHS-LEU-PHE (chain I)
BOC-HIS-PRO-PHE-HIS-LOV-ILE-HIS (chain I)
BOC-HIS-PRO-PHE-HIS-STA-LEU-PHE (chain I)
PRO-HIS-PRO-PHE-HIS-STA-VAL-ILE-HIS-LYS (chain I)
This enzyme belongs to the peptidase family-A1. As it has a catalytic dyad, composed of two aspartic acid residues, it must have a similar mechanism to that of pepsin (D00436 in EzCatDB).
Homology among acid proteases: comparison of crystal structures at 3A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica.
Theoretical calculations on the acidity of the active site in aspartic proteinases.
A Rational Approach to the Design of Antihypertensives. X-Ray Studies of Complexes between Aspartic Proteinases and Aminoalcohol Renin Inhibitors.
X-ray studies of aspartic proteinase-statine inhibitor complexes.
High-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor: the analysis of the inhibitor binding and description of the rigid body shift in the enzyme.
Comparative X-ray crystallographic evidence for a beta-bend conformation as the active structure for peptide T in T4 receptor recognition.
Modulation of the affinity of aspartic proteases by the mutated residues in active site models.
X-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1 A resolution of endothiapepsin.
Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8 A resolution.
X-ray analyses of aspartic proteinases. III Three-dimensional structure of endothiapepsin complexed with a transition-state isostere inhibitor of renin at 1.6 A resolution.
Revised 2.3 A structure of porcine pepsin: evidence for a flexible subdomain.
The active site of aspartic proteinases.
X-ray analysis of a difluorostatone renin inhibitor bound as the tetrahedral hydrate to the aspartic protease endothiapepsin.
A kinetic and equilibrium study of the denaturation of aspartic proteinases from the fungi, Endothia parasitica and Mucor miehei.
X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors.
Synthesis and crystallographic analysis of two rhizopuspepsin inhibitor complexes.
Direct observation by X-ray analysis of the tetrahedral "intermediate" of aspartic proteinases.
Secondary substrate binding in aspartic proteinases: contributions of subsites S3 and S'2 to kcat.
X-ray-crystallographic studies of complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsin.
A quantum mechanical study of the active site of aspartic proteinases.
Extending crystallographic information with semiempirical quantum mechanics and molecular mechanics: a case of aspartic proteinases.
Energy calculations on aspartic proteinases: human renin, endothiapepsin and its complex with an angiotensinogen fragment analogue, H-142.
On the prediction of binding properties of drug molecules by comparative molecular field analysis.
Analyses of ligand binding in five endothiapepsin crystal complexes and their use in the design and evaluation of novel renin inhibitors.
A structural comparison of 21 inhibitor complexes of the aspartic proteinase from Endothia parasitica.
Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin.
A theoretical study of torsional flexibility in the active site of aspartic proteinases: implications for catalysis.
The three-dimensional structure at 2.4 A resolution of glycosylated proteinase A from the lysosome-like vacuole of Saccharomyces cerevisiae.
A fast estimate of electrostatic group contributions to the free energy of protein-inhibitor binding.
Refinement of Four Endothiapepsin Inhibitor Complexes. Crystallographic Studies of Cytochrome Ch from Methylobacterium Extorquens and Inhibitor Complexes of Aspartic Proteinases.
X-ray crystallography (Ph D Thesis 1999 London University Birkbeck College)
Dynamic ligand design and combinatorial optimization: designing inhibitors to endothiapepsin.
A neutron Laue diffraction study of endothiapepsin: implications for the aspartic proteinase mechanism.
The pH dependence of the hydrolysis of chromogenic substrates of the type, Lys-Pro-Xaa-Yaa-Phe-(NO2)Phe-Arg-Leu, by selected aspartic proteinases: evidence for specific interactions in subsites S3 and S2.
Five atomic resolution structures of endothiapepsin inhibitor complexes: implications for the aspartic proteinase mechanism.
The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 A.
Atomic resolution analysis of the catalytic site of an aspartic proteinase and an unexpected mode of binding by short peptides.
Calculating proton uptake/release and binding free energy taking into account ionization and conformation changes induced by protein-inhibitor association: application to plasmepsin, cathepsin D and endothiapepsin-pepstatin complexes.
The structure of a synthetic pepsin inhibitor complexed with endothiapepsin.
The catalytic mechanism of aspartic proteinases.
Crystallographic studies of reduced bond inhibitors complexed with an aspartic proteinase.
Evolution in the structure and function of aspartic proteases.
High resolution X-ray analyses of renin inhibitor-aspartic proteinase complexes.
Domain flexibility in aspartic proteinases.