› 4lp9

X-ray diffraction
1.35Å resolution

Endothiapepsin complexed with Phe-reduced-Tyr peptide.

Released:
DOI: 10.2210/pdb4lp9/pdb
PDB entry 4lp9 coloured by chain, front view.
PDB entry 4lp9 coloured by chain, side view.
PDB entry 4lp9 coloured by chain, top view.
Source organism: Cryphonectria parasitica
Primary publication:
The structure of endothiapepsin complexed with a Phe-Tyr reduced-bond inhibitor at 1.35 Å resolution.
Guo J, Cooper JB, Wood SP
Acta Crystallogr F Struct Biol Commun 70 30-3 (2014)
PMID: 24419612

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145960 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Endothiapepsin Chain: A
Molecule details ›
Chain: A
Length: 330 amino acids
Theoretical weight: 33.81 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
Ser-Leu-Phe-His-Phenylalanyl-reduced-peptide-bond-Tyrosyl-Thr-Pro Chain: I
Molecule details ›
Chain: I
Length: 7 amino acids
Theoretical weight: 998 Da
Source organism: Cryphonectria parasitica
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand SO4 3 x SO4
Ligand GOL 6 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P21
Unit cell:
a: 52.62Å b: 72.787Å c: 45.113Å
α: 90° β: 108.54° γ: 90°
R-values:
R R work R free
0.125 0.123 0.165
Expression system: Not provided

Quick links

Citations

2 mentions without citation

Inherent versus induced protein flexibility: Comparisons within and between apo and holo structures.
Clark et al. (2019)
1 more