PDBe 3v6l

X-ray diffraction
2.2Å resolution

Crystal Structure of caspase-6 inactivation mutation

Released:

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 dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caspase-6 Chains: A, B
Molecule details ›
Chains: A, B
Length: 282 amino acids
Theoretical weight: 32.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55212 (Residues: 21-293; Coverage: 93%)
Gene names: CASP6, MCH2
Sequence domains: Caspase domain
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P6522
Unit cell:
a: 126.35Å b: 126.35Å c: 165.82Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.171 0.169 0.202
Expression system: Escherichia coli