PDBe 4n7j

X-ray diffraction
1.67Å resolution

Tailoring Small Molecules for an Allosteric Site on Procaspase-6

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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caspase-6 Chains: A, B
Molecule details ›
Chains: A, B
Length: 282 amino acids
Theoretical weight: 32.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55212 (Residues: 24-293; Coverage: 92%)
Gene names: CASP6, MCH2
Sequence domains: Caspase domain
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P43212
Unit cell:
a: 116.004Å b: 116.004Å c: 79.532Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.157 0.182
Expression system: Escherichia coli BL21(DE3)