2qzx

X-ray diffraction
2.5Å resolution

Secreted aspartic proteinase (Sap) 5 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:
hetero dimer (preferred)
hetero tetramer
PDBe Complex ID:
PDB-CPX-545317 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Secreted aspartic protease 5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 342 amino acids
Theoretical weight: 37.24 KDa
Source organism: Candida albicans
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P43094 (Residues: 77-418; Coverage: 86%)
Gene names: CAALFM_C603030WA, CaO19.13032, CaO19.5585, SAP5
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
Pepstatin Chains: C, D
Molecule details ›
Chains: C, D
Length: 6 amino acids
Theoretical weight: 686 Da
Source organism: Streptomyces argenteolus subsp. toyonakensis
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P41212
Unit cell:
a: 92.196Å b: 92.196Å c: 182.005Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.246 0.224 0.275
Expression systems:
  • Komagataella pastoris
  • Not provided