PDBe 4fxo

X-ray diffraction
2.85Å resolution

Zinc-mediated allosteric inhibiton of caspase-6

Source organism: Homo sapiens
Primary publication:
Zinc-Mediated Allosteric Inhibition of Caspase-6.
J. Biol. Chem. (2012)
PMID: 22891250

Function and Biology Details

Reaction catalysed:
Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-|-
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Caspase-6 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 299 amino acids
Theoretical weight: 34.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P55212 (Residues: 1-293; Coverage: 100%)
Gene names: CASP6, MCH2
Sequence domains: Caspase domain
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P21
Unit cell:
a: 62.696Å b: 90.855Å c: 85.763Å
α: 90° β: 90.3° γ: 90°
R R work R free
0.216 0.215 0.233
Expression system: Escherichia coli BL21(DE3)