Structure analysis

New crystal structure of yeast Ddi1 aspartyl protease reveals substrate engagement mode

X-ray diffraction
1.8Å resolution
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: 14600 Å2
Buried surface area: 2200 Å2
Dissociation area: 1,100 Å2
Dissociation energy (ΔGdiss): 12 kcal/mol
Dissociation entropy (TΔSdiss): 12 kcal/mol
Interface energy (ΔGint): -19 kcal/mol
Symmetry number: 2

Macromolecules

Chains: A, B
Length: 146 amino acids
Theoretical weight: 16.33 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P40087 (Residues: 185-325; Coverage: 33%)
Gene names: DDI1, VSM1, YER143W
Pfam: gag-polyprotein putative aspartyl protease
InterPro:
CATH: Acid Proteases

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