Structure analysis

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

X-ray diffraction
2.1Å resolution
Source organism: Candida albicans
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 25500 Å2
Buried surface area: 4900 Å2
Dissociation area: 1,100 Å2
Dissociation energy (ΔGdiss): -2 kcal/mol
Dissociation entropy (TΔSdiss): 14 kcal/mol
Interface energy (ΔGint): -9 kcal/mol
Symmetry number: 2

Macromolecules

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: PRA11, PRA2, SAP2
Pfam: Eukaryotic aspartyl protease
InterPro:
CATH: Acid Proteases
SCOP: Pepsin-like

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