› 1epo

X-ray diffraction
2Å resolution

ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN) COMPLEXED WITH CP-81,282 (MOR PHE NLE CHF NME)

Released:
DOI: 10.2210/pdb1epo/pdb
PDB entry 1epo coloured by chain, front view.
PDB entry 1epo coloured by chain, side view.
PDB entry 1epo coloured by chain, top view.
Source organism: Cryphonectria parasitica
Primary publication:
Direct observation by X-ray analysis of the tetrahedral "intermediate" of aspartic proteinases.
Veerapandian B, Cooper JB, Sali A, Blundell TL, Rosati RL, Dominy BW, Damon DB, Hoover DJ
Protein Sci 1 322-8 (1992)
PMID: 1304340

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins with specificity similar to that of pepsin A, prefers hydrophobic residues at P1 and P1', but does not cleave 14-Ala-|-Leu-15 in the B chain of insulin or Z-Glu-Tyr. Clots milk.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145946 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endothiapepsin Chain: E
Molecule details ›
Chain: E
Length: 330 amino acids
Theoretical weight: 33.81 KDa
Source organism: Cryphonectria parasitica
Expression system: Not provided
UniProt:
  • Canonical: P11838 (Residues: 90-419; Coverage: 83%)
Gene names: EAPA, EPN-1
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:
Ligand 2Z3 1 x 2Z3
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 53.7Å b: 73.9Å c: 45.8Å
α: 90° β: 110° γ: 90°
R-values:
R R work R free
0.18 not available not available
Expression system: Not provided

Quick links

Citations

4 review citations

Inhibitors of aspartyl proteinases.
Abdel-Meguid SS. (1993)
3 more

8 mentions without citation

Assessment of programs for ligand binding affinity prediction.
Kim et al. (2008)
7 more