PDBe 1f1j

X-ray diffraction
2.35Å resolution

CRYSTAL STRUCTURE OF CASPASE-7 IN COMPLEX WITH ACETYL-ASP-GLU-VAL-ASP-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:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero octamer
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-7 Chains: A, B
Molecule details ›
Chains: A, B
Length: 305 amino acids
Theoretical weight: 34.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55210 (Residues: 1-303; Coverage: 100%)
Gene names: CASP7, MCH3
Sequence domains: Caspase domain
Structure domains: Rossmann fold
ACE-ASP-GLU-VAL-ASP-CHO Chains: C, D
Molecule details ›
Chains: C, D
Length: 5 amino acids
Theoretical weight: 488 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P3221
Unit cell:
a: 88.18Å b: 88.18Å c: 186.23Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.185 0.263
Expression systems:
  • Escherichia coli
  • Not provided