› 3s70

X-ray diffraction
1.62Å resolution

Crystal structure of active caspase-6 bound with Ac-VEID-CHO solved by As-SAD

Released:
DOI: 10.2210/pdb3s70/pdb
PDB entry 3s70 coloured by chain, front view.
PDB entry 3s70 coloured by chain, side view.
PDB entry 3s70 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Get phases from arsenic anomalous scattering: de novo SAD phasing of two protein structures crystallized in cacodylate buffer.
Liu X, Zhang H, Wang XJ, Li LF, Su XD
PLoS One 6 e24227 (2011)
PMID: 21912678

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:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157273 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-6 Chains: A, C
Molecule details ›
Chains: A, C
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
aldehyde inhibitor Ac-VEID-CHO Chains: B, D
Molecule details ›
Chains: B, D
Length: 5 amino acids
Theoretical weight: 485 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

3 bound ligands:
Ligand CAC 8 x CAC
Ligand ACT 1 x ACT
Ligand MG 1 x MG
1 modified residue:
Ligand ASA 2 x ASA

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P21
Unit cell:
a: 55.39Å b: 89.45Å c: 61.13Å
α: 90° β: 111.7° γ: 90°
R-values:
R R work R free
0.165 0.164 0.194
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

13 citation in other articles

A multipronged approach for compiling a global map of allosteric regulation in the apoptotic caspases.
Dagbay et al. (2014)
12 more

6 mentions without citation

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