PDBe 4jb8

X-ray diffraction
1.7Å resolution

Caspase-7 in Complex with DARPin C7_16

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:
  • not assigned
Biological process:
  • not assigned
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 Chain: A
Molecule details ›
Chain: A
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 Chain: B
Molecule details ›
Chain: B
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 C7_16 Chain: P
Molecule details ›
Chain: P
Length: 171 amino acids
Theoretical weight: 18.2 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: C2
Unit cell:
a: 143.88Å b: 52.51Å c: 60.09Å
α: 90° β: 96.92° γ: 90°
R-values:
R R work R free
0.173 0.172 0.194
Expression system: Escherichia coli