PDBe 1i4o

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE OF THE XIAP/CASPASE-7 COMPLEX

Released:

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:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-7 Chains: A, B
Molecule details ›
Chains: A, B
Length: 280 amino acids
Theoretical weight: 31.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55210 (Residues: 24-303; Coverage: 92%)
Gene names: CASP7, MCH3
Sequence domains: Caspase domain
Structure domains: Rossmann fold
E3 ubiquitin-protein ligase XIAP Chains: C, D
Molecule details ›
Chains: C, D
Length: 141 amino acids
Theoretical weight: 16.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P98170 (Residues: 120-260; Coverage: 28%)
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 F1
Spacegroup: P3221
Unit cell:
a: 88.5Å b: 88.5Å c: 185.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.224 0.224 0.26
Expression system: Escherichia coli