PDBe 4lsz

X-ray diffraction
2.26Å resolution

Caspase-7 in Complex with DARPin D7.18

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:
  • not assigned

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Caspase-7 subunit p20 Chains: A, C
Molecule details ›
Chains: A, C
Length: 175 amino acids
Theoretical weight: 19.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55210 (Residues: 24-198; Coverage: 58%)
Gene names: CASP7, MCH3
Structure domains: Rossmann fold
Caspase-7 subunit p11 Chains: B, D
Molecule details ›
Chains: B, D
Length: 105 amino acids
Theoretical weight: 12.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55210 (Residues: 207-303; Coverage: 32%)
Gene names: CASP7, MCH3
Structure domains: Caspase-like
DARPin D7.18 Chains: E, F
Molecule details ›
Chains: E, F
Length: 169 amino acids
Theoretical weight: 18.3 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
Structure domains: Ankyrin repeat-containing domain

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 59.84Å b: 82.31Å c: 95.08Å
α: 90° β: 91.86° γ: 90°
R-values:
R R work R free
0.176 0.175 0.208
Expression system: Escherichia coli