› 1j71

X-ray diffraction
1.8Å resolution

Structure of the extracellular aspartic proteinase from Candida tropicalis yeast.

Released:
DOI: 10.2210/pdb1j71/pdb
PDB entry 1j71 coloured by chain, front view.
PDB entry 1j71 coloured by chain, side view.
PDB entry 1j71 coloured by chain, top view.
Source organisms:
Primary publication:
High-resolution structure of the extracellular aspartic proteinase from Candida tropicalis yeast.
Symersky J, Monod M, Foundling SI
Biochemistry 36 12700-10 (1997)
PMID: 9335526

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162253 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Candidapepsin Chain: A
Molecule details ›
Chain: A
Length: 334 amino acids
Theoretical weight: 35.95 KDa
Source organism: Candida tropicalis
UniProt:
  • Canonical: Q00663 (Residues: 61-394; Coverage: 90%)
Gene name: SAPT1
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
Tetrapeptide Thr-Ile-Thr-Ser Chain: B
Molecule details ›
Chain: B
Length: 4 amino acids
Theoretical weight: 420 Da
Source organism: unidentified

Ligands and Environments

1 bound ligand:
Ligand EOH 6 x EOH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P212121
Unit cell:
a: 49.96Å b: 51.43Å c: 128.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.165 0.193

Quick links

Citations

5 review citations

Candida glabrata, Candida parapsilosis and Candida tropicalis: biology, epidemiology, pathogenicity and antifungal resistance.
Silva et al. (2012)
4 more

4 mentions without citation

Updates to Binding MOAD (Mother of All Databases): Polypharmacology Tools and Their Utility in Drug Repurposing.
Smith et al. (2019)
3 more