› 2ar9

X-ray diffraction
2.8Å resolution

Crystal structure of a dimeric caspase-9

Released:
DOI: 10.2210/pdb2ar9/pdb
PDB entry 2ar9 coloured by chain, front view.
PDB entry 2ar9 coloured by chain, side view.
PDB entry 2ar9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Engineering a dimeric caspase-9: a re-evaluation of the induced proximity model for caspase activation.
Chao Y, Shiozaki EN, Srinivasula SM, Rigotti DJ, Fairman R, Shi Y
PLoS Biol 3 e183 (2005)
PMID: 15941357

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
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157266 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • 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:
Ligand MLT 1 x MLT
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-values:
R R work R free
0.24 0.237 0.288

Quick links

Citations

25 review citations

Life and death by death receptors.
Guicciardi et al. (2009)
24 more

26 mentions without citation

Small Molecule Active Site Directed Tools for Studying Human Caspases.
Poreba et al. (2015)
25 more