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X-ray diffraction
1.8Å resolution

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

Released:

Function and Biology Details

Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA damage-inducible protein 1 Chains: A, B
Molecule details ›
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
Sequence domains: gag-polyprotein putative aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P212121
Unit cell:
a: 41.515Å b: 50.051Å c: 131.562Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.183 0.213
Expression system: Escherichia coli K-12