PDBe 3v3k

X-ray diffraction
3.49Å resolution

Human caspase 9 in complex with bacterial effector protein

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
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-9 subunit p35 Chains: A, C, E, G, I, K, M, O
Molecule details ›
Chains: A, C, E, G, I, K, M, O
Length: 276 amino acids
Theoretical weight: 30.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55211 (Residues: 141-416; Coverage: 66%)
  • Best match: P55211-2 (Residues: 140-266)
Gene names: CASP9, MCH6
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Effector protein NleF Chains: B, D, F, H, J, L, N, P
Molecule details ›
Chains: B, D, F, H, J, L, N, P
Length: 165 amino acids
Theoretical weight: 18.87 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8XAL7 (Residues: 25-189; Coverage: 87%)
Gene names: ECs1815, Z6020.1, nleF
Sequence domains: NleF caspase inhibitor
Structure domains: Ferritin

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 100.703Å b: 209.906Å c: 317.231Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.248 0.239 0.259
Expression system: Escherichia coli