PDBe 2y0b

X-ray diffraction
2.1Å resolution

Caspase-3 in Complex with an Inhibitory DARPin-3.4_S76R

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:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Caspase-3 subunit p17 Chains: A, C
Molecule details ›
Chains: A, C
Length: 149 amino acids
Theoretical weight: 16.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P42574 (Residues: 29-175; Coverage: 53%)
Gene names: CASP3, CPP32
Structure domains: Rossmann fold
Caspase-3 subunit p12 Chains: B, D
Molecule details ›
Chains: B, D
Length: 118 amino acids
Theoretical weight: 13.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P42574 (Residues: 176-277; Coverage: 37%)
Gene names: CASP3, CPP32
Structure domains: Caspase-like
DARPIN-3.4_S76R Chains: G, H
Molecule details ›
Chains: G, H
Length: 136 amino acids
Theoretical weight: 14.81 KDa
Source organism: unidentified
Expression system: Escherichia coli
Structure domains: Ankyrin repeat-containing domain

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P3121
Unit cell:
a: 98Å b: 98Å c: 192.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.193 0.192 0.217
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli