1se0

X-ray diffraction
1.75Å resolution

Crystal structure of DIAP1 BIR1 bound to a Grim peptide

Released:
Source organism: Drosophila melanogaster
Primary publication:
Molecular mechanisms of DrICE inhibition by DIAP1 and removal of inhibition by Reaper, Hid and Grim.
Nat. Struct. Mol. Biol. 11 420-8 (2004)
PMID: 15107838

Function and Biology Details

Reaction 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
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Death-associated inhibitor of apoptosis 1 Chain: A
Molecule details ›
Chain: A
Length: 116 amino acids
Theoretical weight: 13.55 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
  • Canonical: Q24306 (Residues: 30-145; Coverage: 27%)
Gene names: CG12284, Diap1, Iap1, th
Sequence domains: Inhibitor of Apoptosis domain
Structure domains: Inhibitor Of Apoptosis Protein (2mihbC-IAP-1); Chain A
Cell death protein Grim Chain: B
Molecule details ›
Chain: B
Length: 10 amino acids
Theoretical weight: 1.11 KDa
Source organism: Drosophila melanogaster
Expression system: Not provided
UniProt:
  • Canonical: Q24570 (Residues: 2-11; Coverage: 7%)
Gene names: CG4345, grim

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: R3
Unit cell:
a: 84.783Å b: 84.783Å c: 49.789Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.22 0.212 0.25
Expression systems:
  • Escherichia coli
  • Not provided