› 4iyr

X-ray diffraction
2.7Å resolution

Crystal structure of full-length caspase-6 zymogen

Released:
DOI: 10.2210/pdb4iyr/pdb
PDB entry 4iyr coloured by chain, front view.
PDB entry 4iyr coloured by chain, side view.
PDB entry 4iyr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The regulatory mechanism of the caspase 6 pro-domain revealed by crystal structure and biochemical assays.
Cao Q, Wang XJ, Li LF, Su XD
Acta Crystallogr D Biol Crystallogr 70 58-67 (2014)
PMID: 24419379

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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157270 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caspase-6 Chains: A, B
Molecule details ›
Chains: A, B
Length: 304 amino acids
Theoretical weight: 34.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55212 (Residues: 1-293; Coverage: 100%)
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: SSRF BEAMLINE BL17U
Spacegroup: I4122
Unit cell:
a: 158.062Å b: 158.062Å c: 126.94Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.231
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Activation and regulation of caspase-6 and its role in neurodegenerative diseases.
Wang et al. (2015)
1 more

5 mentions without citation

Small Molecule Active Site Directed Tools for Studying Human Caspases.
Poreba et al. (2015)
4 more