PDBe 3ygs

X-ray diffraction
2.5Å resolution

APAF-1 CARD IN COMPLEX WITH PRODOMAIN OF PROCASPASE-9

Released:

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 dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Apoptotic protease-activating factor 1 Chain: C
Molecule details ›
Chain: C
Length: 95 amino acids
Theoretical weight: 10.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O14727 (Residues: 1-95; Coverage: 8%)
Gene names: APAF1, KIAA0413
Sequence domains: Caspase recruitment domain
Structure domains: Death Domain, Fas
Caspase-9 subunit p35 Chain: P
Molecule details ›
Chain: P
Length: 97 amino acids
Theoretical weight: 11.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55211 (Residues: 1-95; Coverage: 23%)
  • Best match: P55211-4 (Residues: 1-11, 12-12)
Gene names: CASP9, MCH6
Sequence domains: Caspase recruitment domain
Structure domains: Death Domain, Fas

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P6222
Unit cell:
a: 92.5Å b: 92.5Å c: 136.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.224 0.224 0.299
Expression system: Escherichia coli BL21(DE3)