PDBe 4ejf

X-ray diffraction
2.65Å resolution

Allosteric peptides that bind to a caspase zymogen and mediate caspase tetramerization

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 octamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-6 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 279 amino acids
Theoretical weight: 32.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P55212 (Residues: 24-293; Coverage: 92%)
Gene names: CASP6, MCH2
Sequence domains: Caspase domain
Structure domains: Rossmann fold
phage-derived peptide 419 Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 18 amino acids
Theoretical weight: 2.23 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: C2
Unit cell:
a: 128.299Å b: 105.692Å c: 91.924Å
α: 90° β: 106.61° γ: 90°
R-values:
R R work R free
0.191 0.188 0.239
Expression systems:
  • Escherichia coli BL21
  • Not provided