› 3nkf

X-ray diffraction
2.9Å resolution

Crystal structure of human ligand-free mature caspase-6 with intersubunit linker attached

Released:
DOI: 10.2210/pdb3nkf/pdb
PDB entry 3nkf coloured by chain, front view.
PDB entry 3nkf coloured by chain, side view.
PDB entry 3nkf coloured by chain, top view.
Source organism: synthetic construct
Primary publication:
Substrate-induced conformational changes occur in all cleaved forms of caspase-6.
Vaidya S, Velázquez-Delgado EM, Abbruzzese G, Hardy JA
J Mol Biol 406 75-91 (2011)
PMID: 21111746

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

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157270 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caspase-6 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 277 amino acids
Theoretical weight: 31.94 KDa
Source organism: synthetic construct
Expression system: Not provided
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: 63.29Å b: 90.814Å c: 85.912Å
α: 90° β: 91.04° γ: 90°
R-values:
R R work R free
0.219 0.216 0.27
Expression system: Not provided

Quick links

Citations

6 review citations

New approaches for dissecting protease functions to improve probe development and drug discovery.
Deu et al. (2012)
5 more

4 mentions without citation

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