› 2jji

X-ray diffraction
1.57Å resolution

Endothiapepsin in complex with a gem-diol inhibitor.

Released:
DOI: 10.2210/pdb2jji/pdb
PDB entry 2jji coloured by chain, front view.
PDB entry 2jji coloured by chain, side view.
PDB entry 2jji coloured by chain, top view.
Source organism: Cryphonectria parasitica
Primary publication:
The catalytic mechanism of an aspartic proteinase explored with neutron and X-ray diffraction.
Coates L, Tuan HF, Tomanicek S, Kovalevsky A, Mustyakimov M, Erskine P, Cooper J
J Am Chem Soc 130 7235-7 (2008)
PMID: 18479128

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145946 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endothiapepsin Chain: A
Molecule details ›
Chain: A
Length: 329 amino acids
Theoretical weight: 33.8 KDa
Source organism: Cryphonectria parasitica
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 0QS 1 x 0QS
Ligand SO4 1 x SO4
1 modified residue:
Ligand SUI 1 x SUI

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER
Spacegroup: P21
Unit cell:
a: 43.03Å b: 75.72Å c: 42.97Å
α: 90° β: 97.02° γ: 90°
R-values:
R R work R free
0.156 not available 0.196

Quick links

Citations

7 review citations

Neutron crystallography: opportunities, challenges, and limitations.
Blakeley et al. (2008)
6 more

4 mentions without citation

The catalytic mechanism of an aspartic proteinase explored with neutron and X-ray diffraction.
Coates et al. (2008)
3 more