PDBe 3od5

X-ray diffraction
1.6Å resolution

Crystal structure of active caspase-6 bound with Ac-VEID-CHO

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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-6 Chains: A, B
Molecule details ›
Chains: A, B
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
peptide aldehyde inhibitor AC-VEID-CHO Chains: C, D
Molecule details ›
Chains: C, D
Length: 5 amino acids
Theoretical weight: 485 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P21
Unit cell:
a: 55.464Å b: 89.589Å c: 61.145Å
α: 90° β: 111.67° γ: 90°
R-values:
R R work R free
0.156 0.155 0.189
Expression systems:
  • Escherichia coli
  • Not provided