PDBe 1shl

X-ray diffraction
3Å resolution

CASPASE-7 IN COMPLEX WITH FICA ALLOSTERIC INHIBITOR

Released:
Source organism: Homo sapiens
Primary publication:
Discovery of an allosteric site in the caspases.
Proc. Natl. Acad. Sci. U.S.A. 101 12461-6 (2004)
PMID: 15314233

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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caspase-7 subunit p20 Chains: A, B
Molecule details ›
Chains: A, B
Length: 245 amino acids
Theoretical weight: 28.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55210 (Residues: 57-303; Coverage: 78%)
  • Best match: P55210-2 (Residues: 57-149)
Gene names: CASP7, MCH3
Sequence domains: Caspase domain
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P3221
Unit cell:
a: 90.22Å b: 90.22Å c: 186.621Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.224 0.221 0.273
Expression system: Escherichia coli BL21(DE3)