2h6s

X-ray diffraction
2.2Å resolution

Secreted aspartic proteinase (Sap) 3 from Candida albicans

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:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-143567 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Secreted aspartic protease 3 Chain: A
Molecule details ›
Chain: A
Length: 340 amino acids
Theoretical weight: 36.54 KDa
Source organism: Candida albicans
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P0CY29 (Residues: 59-398; Coverage: 90%)
Gene names: CAALFM_C305230WA, CaO19.13422, CaO19.6001, SAP3
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: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P3221
Unit cell:
a: 61.35Å b: 61.35Å c: 171.98Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.258 0.234 0.26
Expression system: Komagataella pastoris