3cvr

X-ray diffraction
2.8Å resolution

Crystal structure of the full length IpaH3

Released:
Primary publication:
Structure of a Shigella effector reveals a new class of ubiquitin ligases.
Nat Struct Mol Biol 15 1302-8 (2008)
PMID: 18997779

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:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-182957 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase ipaH3 Chain: A
Molecule details ›
Chain: A
Length: 571 amino acids
Theoretical weight: 65.51 KDa
Source organism: Shigella flexneri 2a str. 301
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q83RJ4 (Residues: 1-571; Coverage: 100%)
Gene names: SF1383, ipaH3
Sequence domains:
Structure domains: Ribonuclease Inhibitor

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 3W1A, PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P41212
Unit cell:
a: 154.19Å b: 154.19Å c: 85.87Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.252 0.251 0.277
Expression system: Escherichia coli BL21