4jj8

X-ray diffraction
2.94Å resolution

Caspase-3 specific unnatural amino acid peptides

Released:

Function and Biology Details

Reaction catalysed:
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157232 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-7 subunit p20 Chains: A, B
Molecule details ›
Chains: A, B
Length: 255 amino acids
Theoretical weight: 29.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55210 (Residues: 57-303; Coverage: 82%)
Gene names: CASP7, MCH3
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Caspase Inhibitor Chains: C, D
Molecule details ›
Chains: C, D
Length: 6 amino acids
Theoretical weight: 823 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P3221
Unit cell:
a: 89.089Å b: 89.089Å c: 185.535Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.193 0.216
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided