PDBe 1eag

X-ray diffraction
2.1Å resolution

Secreted aspartic proteinase (SAP2) from Candida albicans complexed with A70450

Released:

Function and Biology Details

Reaction catalysed:
Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades keratin. 
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Candidapepsin-2 Chain: A
Molecule details ›
Chain: A
Length: 342 amino acids
Theoretical weight: 36.36 KDa
Source organism: Candida albicans
UniProt:
  • Canonical: P0CS83 (Residues: 57-398; Coverage: 90%)
Gene names: PRA11, PRA2, SAP2
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 76.2Å b: 76.2Å c: 126.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.268