› 1pyo

X-ray diffraction
1.65Å resolution

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

Released:
DOI: 10.2210/pdb1pyo/pdb
PDB entry 1pyo coloured by chain, front view.
PDB entry 1pyo coloured by chain, side view.
PDB entry 1pyo coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway.
Schweizer A, Briand C, Grutter MG
J Biol Chem 278 42441-7 (2003)
PMID: 12920126

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:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153126 (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
Sequence domains: Caspase domain
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
Sequence domains: Caspase domain
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

Quick links

Citations

22 review citations

Molecular mechanisms of caspase regulation during apoptosis.
Riedl et al. (2004)
21 more

16 mentions without citation

Small Molecule Active Site Directed Tools for Studying Human Caspases.
Poreba et al. (2015)
15 more