› 3v6m

X-ray diffraction
2.69Å resolution

Inhibition of caspase-6 activity by single mutation outside the active site

Released:
DOI: 10.2210/pdb3v6m/pdb
PDB entry 3v6m coloured by chain, front view.
PDB entry 3v6m coloured by chain, side view.
PDB entry 3v6m coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Inhibitory mechanism of caspase-6 phosphorylation revealed by crystal structures, molecular dynamics simulations, and biochemical assays.
Cao Q, Wang XJ, Liu CW, Liu DF, Li LF, Gao YQ, Su XD
J Biol Chem 287 15371-9 (2012)
PMID: 22433863

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, C, D, F, G, I, J
Molecule details ›
Chains: A, B, C, D, F, G, I, J
Length: 279 amino acids
Theoretical weight: 32.23 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: SSRF BEAMLINE BL17U
Spacegroup: P21
Unit cell:
a: 81.146Å b: 162.63Å c: 89.15Å
α: 90° β: 95.01° γ: 90°
R-values:
R R work R free
0.217 0.215 0.259
Expression system: Escherichia coli

Quick links

Citations

6 review citations

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

1 mention without citation

Inhibitory mechanism of caspase-6 phosphorylation revealed by crystal structures, molecular dynamics simulations, and biochemical assays.
Cao et al. (2012)