› 1eag

X-ray diffraction
2.1Å resolution

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

Released:
DOI: 10.2210/pdb1eag/pdb
PDB entry 1eag coloured by chain, front view.
PDB entry 1eag coloured by chain, side view.
PDB entry 1eag coloured by chain, top view.
Source organism: Candida albicans
Primary publication:
The crystal structure of a major secreted aspartic proteinase from Candida albicans in complexes with two inhibitors.
Cutfield SM, Dodson EJ, Anderson BF, Moody PC, Marshall CJ, Sullivan PA, Cutfield JF
Structure 3 1261-71 (1995)
PMID: 8591036

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143549 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Secreted aspartic protease 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: PEP11, PRA11, SAP2
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:
Ligand A70 1 x A70
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

Quick links

Citations

14 review citations

Candida albicans secreted aspartyl proteinases in virulence and pathogenesis.
Naglik et al. (2003)
13 more

7 mentions without citation

Candida albicans possesses Sap7 as a pepstatin A-insensitive secreted aspartic protease.
Aoki et al. (2012)
6 more