› 1k86

X-ray diffraction
2.6Å resolution

Crystal structure of caspase-7

Released:
DOI: 10.2210/pdb1k86/pdb
PDB entry 1k86 coloured by chain, front view.
PDB entry 1k86 coloured by chain, side view.
PDB entry 1k86 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of a procaspase-7 zymogen: mechanisms of activation and substrate binding.
Chai J, Wu Q, Shiozaki E, Srinivasula SM, Alnemri ES, Shi Y
Cell 107 399-407 (2001)
PMID: 11701129

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
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157233 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caspase-7 subunit p20 Chains: A, B
Molecule details ›
Chains: A, B
Length: 253 amino acids
Theoretical weight: 28.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55210 (Residues: 51-303; Coverage: 84%)
Gene names: CASP7, MCH3
Sequence domains: Caspase domain
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P3221
Unit cell:
a: 88.9Å b: 88.9Å c: 186.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.234 0.232 0.257
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

38 review citations

Molecular mechanisms of caspase regulation during apoptosis.
Riedl et al. (2004)
37 more

15 mentions without citation

The protein structures that shape caspase activity, specificity, activation and inhibition.
Fuentes-Prior et al. (2004)
14 more