PDBe 3nr2

X-ray diffraction
2.9Å resolution

Crystal structure of Caspase-6 zymogen

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: 294 amino acids
Theoretical weight: 33.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55212 (Residues: 24-293; Coverage: 92%)
  • Best match: P55212-2 (Residues: 14-204)
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: BRUKER AXS MICROSTAR-H
Spacegroup: P6522
Unit cell:
a: 127.983Å b: 127.983Å c: 167.912Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.179 0.237
Expression system: Escherichia coli