PDBe 3r6g

X-ray diffraction
2.07Å resolution

Crystal structure of active caspase-2 bound with Ac-VDVAD-CHO

Released:
Source organism: Homo sapiens

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-|-
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero trimer (preferred)
hetero hexamer
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Caspase-2 subunit p18 Chains: A, C
Molecule details ›
Chains: A, C
Length: 160 amino acids
Theoretical weight: 18.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P42575 (Residues: 175-333; Coverage: 35%)
Gene names: CASP2, ICH1, NEDD2
Structure domains: Rossmann fold
Caspase-2 subunit p12 Chains: B, D
Molecule details ›
Chains: B, D
Length: 112 amino acids
Theoretical weight: 12.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P42575 (Residues: 349-452; Coverage: 23%)
Gene names: CASP2, ICH1, NEDD2
Structure domains: Caspase-like
Peptide Inhibitor (ACE)VDVAD-CHO Chains: E, F
Molecule details ›
Chains: E, F
Length: 6 amino acids
Theoretical weight: 528 Da

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P212121
Unit cell:
a: 63.322Å b: 97.692Å c: 96.856Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.167 0.21
Expression system: Escherichia coli