PDBe 3r5k

X-ray diffraction
2.86Å resolution

A designed redox-controlled caspase-7

Released:
Source organism: Homo sapiens
Primary publication:
A designed redox-controlled caspase.
Protein Sci. (2011)
PMID: 21674661

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 312 amino acids
Theoretical weight: 35.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55210 (Residues: 1-198, 199-303; Coverage: 100%)
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 24-ID-C
Spacegroup: P3221
Unit cell:
a: 89.85Å b: 89.85Å c: 185.91Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.188 0.251
Expression system: Escherichia coli BL21(DE3)