Structure analysis

Automated refinement of diffraction data obtained from an endothiapepsin crystal treated with fragment 228

X-ray diffraction
1.12Å resolution
Source organism: Cryphonectria parasitica
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 12830.89 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-145946

Macromolecules

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
Pfam: Eukaryotic aspartyl protease
InterPro:
CATH: Acid Proteases

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