PDBe 1nms

X-ray diffraction
1.7Å resolution

Caspase-3 tethered to irreversible inhibitor

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
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caspase-3 subunit p17 Chains: A, B
Molecule details ›
Chains: A, B
Length: 249 amino acids
Theoretical weight: 28.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P42574 (Residues: 29-277; Coverage: 90%)
Gene names: CASP3, CPP32
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: SSRL BEAMLINE BL7-1
Spacegroup: C2
Unit cell:
a: 123.45Å b: 70.952Å c: 95.86Å
α: 90° β: 136.42° γ: 90°
R-values:
R R work R free
0.153 0.151 0.183
Expression system: Escherichia coli