› 1gqf

X-ray diffraction
2.9Å resolution

Crystal structure of human procaspase-7

Released:
DOI: 10.2210/pdb1gqf/pdb
PDB entry 1gqf coloured by chain, front view.
PDB entry 1gqf coloured by chain, side view.
PDB entry 1gqf coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the activation of human procaspase-7.
Riedl SJ, Fuentes-Prior P, Renatus M, Kairies N, Krapp S, Huber R, Salvesen GS, Bode W
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:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157233 (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:
Ligand SO4 5 x SO4
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

Quick links

Citations

29 review citations

Molecular mechanisms of caspase regulation during apoptosis.
Riedl et al. (2004)
28 more

17 mentions without citation

The protein structures that shape caspase activity, specificity, activation and inhibition.
Fuentes-Prior et al. (2004)
16 more