3tne

X-ray diffraction
2.4Å resolution

The crystal structure of protease Sapp1p from Candida parapsilosis in complex with the HIV protease inhibitor ritonavir

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.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Candidapepsin-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 339 amino acids
Theoretical weight: 35.87 KDa
Source organism: Candida parapsilosis
UniProt:
  • Canonical: P32951 (Residues: 63-402; Coverage: 90%)
Gene names: ACPR, SAPP1
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
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P212121
Unit cell:
a: 61.87Å b: 61.61Å c: 157.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.257 0.254 0.317