PDBe 3ibc

X-ray diffraction
2.75Å resolution

Crystal Structure of Caspase-7 incomplex with Acetyl-YVAD-CHO

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:
  • 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-7 subunit p20 Chains: A, C
Molecule details ›
Chains: A, C
Length: 173 amino acids
Theoretical weight: 19.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55210 (Residues: 24-196; Coverage: 57%)
Gene names: CASP7, MCH3
Structure domains: Rossmann fold
Caspase-7 subunit p11 Chains: B, D
Molecule details ›
Chains: B, D
Length: 97 amino acids
Theoretical weight: 11.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55210 (Residues: 207-303; Coverage: 32%)
Gene names: CASP7, MCH3
Structure domains: Caspase-like
Acetyl-YVAD-CHO Chains: E, F
Molecule details ›
Chains: E, F
Length: 5 amino acids
Theoretical weight: 493 Da

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P3221
Unit cell:
a: 88.248Å b: 88.248Å c: 188.15Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.216 0.203 0.242
Expression system: Escherichia coli