PDBe 1gqf

X-ray diffraction
2.9Å resolution

Crystal structure of human procaspase-7

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for the activation of human procaspase-7.
Proc. Natl. Acad. Sci. U.S.A. 98 14790-5 (2001)
PMID: 11752425

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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Caspase-7 subunit p20 Chains: A, B
Molecule details ›
Chains: A, B
Length: 265 amino acids
Theoretical weight: 30.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55210 (Residues: 47-303; Coverage: 85%)
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: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P3221
Unit cell:
a: 90.21Å b: 90.21Å c: 183.02Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.268 0.268 0.285
Expression system: Escherichia coli