› 1epr

X-ray diffraction
2.3Å resolution

ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN) COMPLEXED WITH PD-135,040

Released:
DOI: 10.2210/pdb1epr/pdb
PDB entry 1epr coloured by chain, front view.
PDB entry 1epr coloured by chain, side view.
PDB entry 1epr coloured by chain, top view.
Source organism: Cryphonectria parasitica
Primary publication:
A structural comparison of 21 inhibitor complexes of the aspartic proteinase from Endothia parasitica.
Bailey D, Cooper JB
Protein Sci 3 2129-43 (1994)
PMID: 7703859

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 0QS 1 x 0QS
1 modified residue:
Ligand DGN 1 x DGN

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 43.09Å b: 75.77Å c: 43.01Å
α: 90° β: 97° γ: 90°
R-values:
R R work R free
0.181 not available not available
Expression system: Not provided

Quick links

Citations

17 citation in other articles

Structural basis for inhibition of Aspergillus niger xylanase by triticum aestivum xylanase inhibitor-I.
Sansen et al. (2004)
16 more

1 mention without citation

Detection of cave pockets in large molecules: Spaces into which internal probes can enter, but external probes from outside cannot.
Kawabata T. (2019)