PDBe 4rhw

X-ray diffraction
2.1Å resolution

Crystal structure of Apaf-1 CARD and caspase-9 CARD complex

Released:
Source organism: Homo sapiens
Primary publication:
Molecular determinants of caspase-9 activation by the Apaf-1 apoptosome.
Proc. Natl. Acad. Sci. U.S.A. 111 16254-61 (2014)
PMID: 25313070

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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Apoptotic protease-activating factor 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 97 amino acids
Theoretical weight: 11.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O14727 (Residues: 1-97; Coverage: 8%)
Gene names: APAF1, KIAA0413
Sequence domains: Caspase recruitment domain
Structure domains: Death Domain, Fas
Caspase-9 subunit p35 Chains: E, F
Molecule details ›
Chains: E, F
Length: 108 amino acids
Theoretical weight: 12.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55211 (Residues: 1-100; Coverage: 24%)
Gene names: CASP9, MCH6
Sequence domains: Caspase recruitment domain
Structure domains: Death Domain, Fas

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 64.531Å b: 92.52Å c: 68.031Å
α: 90° β: 109.12° γ: 90°
R-values:
R R work R free
0.211 0.21 0.226
Expression system: Escherichia coli