PDBe 1jxq

X-ray diffraction
2.8Å resolution

Structure of cleaved, CARD domain deleted Caspase-9

Released:
Source organism: Homo sapiens
Primary publication:
Dimer formation drives the activation of the cell death protease caspase 9.
Proc. Natl. Acad. Sci. U.S.A. 98 14250-5 (2001)
PMID: 11734640

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:
hetero trimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-9 subunit p35 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 284 amino acids
Theoretical weight: 31.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55211 (Residues: 139-416; Coverage: 67%)
  • Best match: P55211-2 (Residues: 140-266)
Gene names: CASP9, MCH6
Sequence domains: Caspase domain
Structure domains: Rossmann fold
benzoxycarbonyl-Val-Ala-Asp-fluoromethyl ketone Inhibitor Chains: E, F
Molecule details ›
Chains: E, F
Length: 5 amino acids
Theoretical weight: 530 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: C2
Unit cell:
a: 144.3Å b: 81.8Å c: 125.4Å
α: 90° β: 111.7° γ: 90°
R-values:
R R work R free
0.233 0.233 0.275
Expression systems:
  • Escherichia coli
  • Not provided