› 4lbt

X-ray diffraction
1.25Å resolution

Endothiapepsin in complex with 100mM acylhydrazone inhibitor

Released:
DOI: 10.2210/pdb4lbt/pdb
PDB entry 4lbt coloured by chain, front view.
PDB entry 4lbt coloured by chain, side view.
PDB entry 4lbt coloured by chain, top view.
Source organism: Cryphonectria parasitica
Primary publication:
Structure-based design of inhibitors of the aspartic protease endothiapepsin by exploiting dynamic combinatorial chemistry.
Mondal M, Radeva N, Köster H, Park A, Potamitis C, Zervou M, Klebe G, Hirsch AK
Angew Chem Int Ed Engl 53 3259-63 (2014)
PMID: 24532096

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: 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

Ligands and Environments

3 bound ligands:
Ligand DMS 1 x DMS
Ligand 1TZ 3 x 1TZ
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P21
Unit cell:
a: 45.428Å b: 72.933Å c: 52.961Å
α: 90° β: 109.3° γ: 90°
R-values:
R R work R free
0.123 0.122 0.139

Quick links

Citations

9 review citations

Applying thermodynamic profiling in lead finding and optimization.
Klebe G. (2015)
8 more