› 9g34

X-ray diffraction
1.3Å resolution

The HIV protease inhibitor darunavir binding to the active site of Cryphonectria parasitica endothiapepsin

Released:
DOI: 10.2210/pdb9g34/pdb
PDB entry 9g34 coloured by chain, front view.
PDB entry 9g34 coloured by chain, side view.
PDB entry 9g34 coloured by chain, top view.
Source organism: Cryphonectria parasitica
Entry authors: Falke S, Senst JM, Guenther S, Meents A

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145946 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endothiapepsin Chains: A, B
Molecule details ›
Chains: A, B
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

Ligands and Environments

4 bound ligands:
Ligand 017 2 x 017
Ligand DMS 2 x DMS
Ligand NA 2 x NA
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, DESY BEAMLINE P11
Spacegroup: P21
Unit cell:
a: 45.654Å b: 72.336Å c: 101.942Å
α: 90° β: 95.873° γ: 90°
R-values:
R R work R free
0.158 0.158 0.172

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