› 4ybf

X-ray diffraction
1.24Å resolution

Aspartic Proteinase Sapp2 Secreted from Candida Parapsilosis at 1.25 A Resolution

Released:
DOI: 10.2210/pdb4ybf/pdb
PDB entry 4ybf coloured by chain, front view.
PDB entry 4ybf coloured by chain, side view.
PDB entry 4ybf coloured by chain, top view.
Source organism: Candida parapsilosis CDC317
Primary publication:
Atomic resolution crystal structure of Sapp2p, a secreted aspartic protease from Candida parapsilosis.
Dostál J, Pecina A, Hrušková-Heidingsfeldová O, Marečková L, Pichová I, Řezáčová P, Lepšík M, Brynda J
Acta Crystallogr D Biol Crystallogr 71 2494-504 (2015)
PMID: 26627656

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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124591 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
candidapepsin Chain: A
Molecule details ›
Chain: A
Length: 334 amino acids
Theoretical weight: 35.47 KDa
Source organism: Candida parapsilosis CDC317
Expression system: Candida parapsilosis
UniProt:
  • Canonical: G8B6Y8 (Residues: 72-405; Coverage: 83%)
Gene names: CPAR2_102580, SAPP2
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P21
Unit cell:
a: 49.138Å b: 57.147Å c: 54.553Å
α: 90° β: 90.61° γ: 90°
R-values:
R R work R free
0.148 0.147 0.174
Expression system: Candida parapsilosis

Quick links

Citations

1 review citation

Extracellular proteinases of Candida species pathogenic yeasts.
Rapala-Kozik et al. (2018)
5 other articles

1 mention without citation

Partial Characterization of Two Cathepsin D Family Aspartic Peptidases of Clonorchis sinensis.
Kang et al. (2019)