PDBe 1nme

X-ray diffraction
1.6Å resolution

Structure of Casp-3 with tethered salicylate

Released:

Function and Biology Details

Reaction catalysed:
Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero octamer
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-3 subunit p17 Chain: A
Molecule details ›
Chain: A
Length: 146 amino acids
Theoretical weight: 16.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P42574 (Residues: 29-174; Coverage: 53%)
Gene names: CASP3, CPP32
Structure domains: Rossmann fold
Caspase-3 subunit p12 Chain: B
Molecule details ›
Chain: B
Length: 92 amino acids
Theoretical weight: 10.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P42574 (Residues: 186-277; Coverage: 33%)
Gene names: CASP3, CPP32
Structure domains: Caspase-like

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: I222
Unit cell:
a: 69.488Å b: 83.598Å c: 95.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.172 0.205
Expression system: Escherichia coli