1nw9

X-ray diffraction
2.4Å resolution

STRUCTURE OF CASPASE-9 IN AN INHIBITORY COMPLEX WITH XIAP-BIR3

Released:
Source organism: Homo sapiens

Function and Biology Details

Reactions catalysed:
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
Strict requirement for an Asp residue at position P1 and with a marked preference for His at position P2. It has a preferred cleavage sequence of Leu-Gly-His-Asp-|-Xaa
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157263 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase XIAP Chain: A
Molecule details ›
Chain: A
Length: 98 amino acids
Theoretical weight: 11.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P98170 (Residues: 253-350; Coverage: 20%)
Gene names: API3, BIRC4, IAP3, XIAP
Sequence domains: Inhibitor of Apoptosis domain
Structure domains: Inhibitor Of Apoptosis Protein (2mihbC-IAP-1); Chain A
Caspase-9 subunit p35 Chain: B
Molecule details ›
Chain: B
Length: 277 amino acids
Theoretical weight: 30.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55211 (Residues: 140-416; Coverage: 67%)
Gene names: CASP9, MCH6
Sequence domains: Caspase domain
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P6522
Unit cell:
a: 104.4Å b: 104.4Å c: 170.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.23 0.23 0.235
Expression system: Escherichia coli