› 3t6p

X-ray diffraction
1.9Å resolution

IAP antagonist-induced conformational change in cIAP1 promotes E3 ligase activation via dimerization

Released:
DOI: 10.2210/pdb3t6p/pdb
PDB entry 3t6p coloured by chain, front view.
PDB entry 3t6p coloured by chain, side view.
PDB entry 3t6p coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination.
Dueber EC, Schoeffler AJ, Lingel A, Elliott JM, Fedorova AV, Giannetti AM, Zobel K, Maurer B, Varfolomeev E, Wu P, Wallweber HJ, Hymowitz SG, Deshayes K, Vucic D, Fairbrother WJ
Science 334 376-80 (2011)
PMID: 22021857

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:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171717 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Baculoviral IAP repeat-containing protein 2 Chain: A
Molecule details ›
Chain: A
Length: 345 amino acids
Theoretical weight: 39.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13490 (Residues: 265-618; Coverage: 56%)
Gene names: API1, BIRC2, MIHB, RNF48
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P212121
Unit cell:
a: 37.971Å b: 85.432Å c: 106.484Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.191 0.233
Expression system: Escherichia coli

Quick links

Citations

51 review citations

Ubiquitin Ligases: Structure, Function, and Regulation.
Zheng et al. (2017)
50 more

9 mentions without citation

Inhibitor of apoptosis (IAP) proteins-modulators of cell death and inflammation.
Silke et al. (2013)
8 more