PDBe 4fea

X-ray diffraction
3.79Å resolution

Crystal structure of CASPASE-7 in Complex with allosteric inhibitor

Released:

Function and Biology Details

Reaction catalysed:
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caspase-7 subunit p20 Chains: A, B
Molecule details ›
Chains: A, B
Length: 247 amino acids
Theoretical weight: 28.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55210 (Residues: 57-303; Coverage: 82%)
Gene names: CASP7, MCH3
Sequence domains: Caspase domain
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P3221
Unit cell:
a: 88.72Å b: 88.72Å c: 185.66Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.242 0.236 0.286
Expression system: Escherichia coli