PDBe 3rjm

X-ray diffraction
2.55Å resolution

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
Molecule details ›
Chains: A, C
Length: 169 amino acids
Theoretical weight: 18.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P42575 (Residues: 167-333; Coverage: 37%)
Gene names: CASP2, ICH1, NEDD2
Caspase-2 subunit p12 Chains: B, D
Molecule details ›
Chains: B, D
Length: 117 amino acids
Theoretical weight: 13.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P42575 (Residues: 348-452; Coverage: 23%)
Gene names: CASP2, ICH1, NEDD2
Structure domains: Caspase-like
Peptide inhibitor (ACE)VDV(3PX)D-CHO Chains: E, F
Molecule details ›
Chains: E, F
Length: 6 amino acids
Theoretical weight: 614 Da

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P212121
Unit cell:
a: 63.77Å b: 97.38Å c: 97.98Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.186 0.249
Expression system: Escherichia coli BL21(DE3)