› 1ent

X-ray diffraction
1.9Å resolution

X-RAY ANALYSES OF ASPARTIC PROTEINASES. THE THREE-DIMENSIONAL STRUCTURE AT 2.1 ANGSTROMS RESOLUTION OF ENDOTHIAPEPSIN

Released:
DOI: 10.2210/pdb1ent/pdb
PDB entry 1ent coloured by chain, front view.
PDB entry 1ent coloured by chain, side view.
PDB entry 1ent coloured by chain, top view.
Source organism: Cryphonectria parasitica
Primary publication:
X-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1 A resolution of endothiapepsin.
Blundell TL, Jenkins JA, Sewell BT, Pearl LH, Cooper JB, Tickle IJ, Veerapandian B, Wood SP
J Mol Biol 211 919-41 (1990)
PMID: 2179568

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

2 bound ligands:
Ligand 0EM 1 x 0EM
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 43Å b: 75.7Å c: 42.9Å
α: 90° β: 97.1° γ: 90°
R-values:
R R work R free
0.17 not available not available
Expression system: Not provided

Quick links

Citations

5 review citations

The structure and function of Saccharomyces cerevisiae proteinase A.
Parr et al. (2007)
4 more

1 mention without citation

Automated site preparation in physics-based rescoring of receptor ligand complexes.
Rapp et al. (2009)