PDBe 3k7e

X-ray diffraction
3Å resolution

Crystal structure of human ligand-free mature caspase-6

Released:
Source organism: Homo sapiens
Entry authors: Vaidya S, Hardy JA

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
Macromolecule:
Caspase-6 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 278 amino acids
Theoretical weight: 32.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55212 (Residues: 24-293; Coverage: 92%)
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: NSLS BEAMLINE X6A
Spacegroup: P21
Unit cell:
a: 63.394Å b: 90.944Å c: 86.202Å
α: 90° β: 91.46° γ: 90°
R-values:
R R work R free
0.221 0.218 0.259
Expression system: Escherichia coli