PDBe 1pyo

X-ray diffraction
1.65Å resolution

Crystal Structure of Human Caspase-2 in Complex with Acetyl-Leu-Asp-Glu-Ser-Asp-cho

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
Molecule details ›
Chains: A, C
Length: 167 amino acids
Theoretical weight: 18.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P42575 (Residues: 167-333; Coverage: 37%)
Gene names: CASP2, ICH1, NEDD2
Structure domains: Rossmann fold
Caspase-2 subunit p12 Chains: B, D
Molecule details ›
Chains: B, D
Length: 105 amino acids
Theoretical weight: 11.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P42575 (Residues: 348-452; Coverage: 23%)
Gene names: CASP2, ICH1, NEDD2
Structure domains: Caspase-like
IML2-like protein YKR018C Chains: E, F
Molecule details ›
Chains: E, F
Length: 6 amino acids
Theoretical weight: 590 Da
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
UniProt:
  • Canonical: P36114 (Residues: 54-57; Coverage: 1%)
Gene name: YKR018C

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 63.649Å b: 96.583Å c: 97.547Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.213
Expression systems:
  • Escherichia coli
  • Not provided