PDBe 2p2c

X-ray diffraction
3.24Å resolution

Inhibition of caspase-2 by a designed ankyrin repeat protein (DARPin)

Released:

Function and Biology Details

Reaction catalysed:
Strict requirement for an Asp residue at P1, with 316-asp being essential for proteolytic activity and has a preferred cleavage sequence of Val-Asp-Val-Ala-Asp-|-
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Caspase-2 subunit p18 Chains: A, C, E, G, I, K
Molecule details ›
Chains: A, C, E, G, I, K
Length: 169 amino acids
Theoretical weight: 19.01 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P42575 (Residues: 167-333; Coverage: 37%)
Gene names: CASP2, ICH1, NEDD2
Structure domains: Rossmann fold
Caspase-2 subunit p12 Chains: B, D, F, H, J, L
Molecule details ›
Chains: B, D, F, H, J, L
Length: 106 amino acids
Theoretical weight: 12.05 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P42575 (Residues: 348-452; Coverage: 23%)
Gene names: CASP2, ICH1, NEDD2
Structure domains: Caspase-like
Caspase-2 Chains: P, Q, R, S, T, U
Molecule details ›
Chains: P, Q, R, S, T, U
Length: 169 amino acids
Theoretical weight: 18.44 KDa
Source organism: Homo sapiens
Expression system: Not provided
Structure domains: Ankyrin repeat-containing domain

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 58.02Å b: 229.21Å c: 114.93Å
α: 90° β: 90.11° γ: 90°
R-values:
R R work R free
0.262 0.262 0.305
Expression system: Not provided