PDBe 1i51

X-ray diffraction
2.45Å resolution

CRYSTAL STRUCTURE OF CASPASE-7 COMPLEXED WITH XIAP

Released:
Source organism: Homo sapiens

Function and Biology Details

Reactions catalysed:
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
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: 148 amino acids
Theoretical weight: 16.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55210 (Residues: 51-198; Coverage: 49%)
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: 12.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P55210 (Residues: 199-303; Coverage: 35%)
Gene names: CASP7, MCH3
Structure domains: Caspase-like
E3 ubiquitin-protein ligase XIAP Chains: E, F
Molecule details ›
Chains: E, F
Length: 117 amino acids
Theoretical weight: 13.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P98170 (Residues: 124-240; Coverage: 24%)
Gene names: API3, BIRC4, IAP3, XIAP
Sequence domains: Inhibitor of Apoptosis domain

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P3221
Unit cell:
a: 89.6Å b: 89.6Å c: 185.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.235 0.233 0.272
Expression system: Escherichia coli BL21(DE3)