X-ray diffraction
2.8Å resolution

Crystal structure of a dimeric caspase-9


Function and Biology Details

Reaction catalysed:
Strict requirement for an Asp residue at position P1 and with a marked preference for His at position P2. It has a preferred cleavage sequence of Leu-Gly-His-Asp-|-Xaa
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Caspase-9 subunit p35 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 278 amino acids
Theoretical weight: 30.55 KDa
Source organism: Homo sapiens
  • Canonical: P55211 (Residues: 139-416; Coverage: 67%)
Gene names: CASP9, MCH6
Sequence domains: Caspase domain
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 144.698Å b: 78.055Å c: 125.963Å
α: 90° β: 112.5° γ: 90°
R R work R free
0.24 0.237 0.288