PDBe 4hqr

X-ray diffraction
3Å resolution

Crystal Structure of mutant form of Caspase-7

Released:
Source organism: Homo sapiens
Primary publication:
Structural asymmetry of procaspase-7 bound to a specific inhibitor.
Acta Crystallogr. D Biol. Crystallogr. 69 1514-21 (2013)
PMID: 23897474

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 tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-7 subunit p20 Chains: A, B
Molecule details ›
Chains: A, B
Length: 272 amino acids
Theoretical weight: 31.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55210 (Residues: 47-204, 205-303; Coverage: 85%)
  • Best match: P55210-2 (Residues: 47-149)
Gene names: CASP7, MCH3
Sequence domains: Caspase domain
Structure domains: Rossmann fold
Ac-Asp-Glu-Val-Asp-Aldehyde Chains: E, F
Molecule details ›
Chains: E, F
Length: 5 amino acids
Theoretical weight: 488 Da

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 6C1
Spacegroup: P3221
Unit cell:
a: 90.48Å b: 90.48Å c: 185.05Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.221 0.218 0.253
Expression system: Escherichia coli