› 1oex

X-ray diffraction
1.1Å resolution

Atomic Resolution Structure of Endothiapepsin in Complex with a Hydroxyethylene Transition State Analogue Inhibitor H261

Released:
DOI: 10.2210/pdb1oex/pdb
PDB entry 1oex coloured by chain, front view.
PDB entry 1oex coloured by chain, side view.
PDB entry 1oex coloured by chain, top view.
Source organisms:
Primary publication:
Atomic resolution analysis of the catalytic site of an aspartic proteinase and an unexpected mode of binding by short peptides.
Erskine PT, Coates L, Mall S, Gill RS, Wood SP, Myles DA, Cooper JB
Protein Sci 12 1741-9 (2003)
PMID: 12876323

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145951 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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
INHIBITOR H261 Chain: B
Molecule details ›
Chain: B
Length: 8 amino acids
Theoretical weight: 1.04 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand GOL 1 x GOL
Ligand SO4 4 x SO4
1 modified residue:
Ligand SUI 1 x SUI

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P21
Unit cell:
a: 42.58Å b: 74.51Å c: 42.35Å
α: 90° β: 97.56° γ: 90°
R-values:
R R work R free
0.14 not available 0.178
Expression system: Not provided

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Citations

1 review citation

Structural studies of vacuolar plasmepsins.
Bhaumik et al. (2012)
8 other articles

5 mentions without citation

How similar are enzyme active site geometries derived from quantum mechanical theozymes to crystal structures of enzyme-inhibitor complexes? Implications for enzyme design.
Dechancie et al. (2007)
4 more