› 4ejf

X-ray diffraction
2.65Å resolution

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

Released:
DOI: 10.2210/pdb4ejf/pdb
PDB entry 4ejf coloured by chain, front view.
PDB entry 4ejf coloured by chain, side view.
PDB entry 4ejf coloured by chain, top view.
Source organisms:
Primary publication:
Allosteric peptides bind a caspase zymogen and mediate caspase tetramerization.
Stanger K, Steffek M, Zhou L, Pozniak CD, Quan C, Franke Y, Tom J, Tam C, Krylova I, Elliott JM, Lewcock JW, Zhang Y, Murray J, Hannoush RN
Nat Chem Biol 8 655-60 (2012)
PMID: 22683611

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 octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157277 (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:
Ligand PO4 2 x PO4
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

Quick links

Citations

6 review citations

Expanding the number of 'druggable' targets: non-enzymes and protein-protein interactions.
Makley et al. (2013)
5 more

1 mention without citation

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