3ckd

X-ray diffraction
2.65Å resolution

Crystal structure of the C-terminal domain of the Shigella type III effector IpaH

Released:

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
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-148257 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase ipaH7.8 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 312 amino acids
Theoretical weight: 35.64 KDa
Source organism: Shigella flexneri 2a str. 301
Expression system: Escherichia coli
UniProt:
  • Canonical: P18014 (Residues: 255-273, 274-560; Coverage: 54%)
Gene names: CP0078, SFLP133, ipaH7.8, pWR501_0084
Sequence domains: C-terminal novel E3 ligase, LRR-interacting
Structure domains:

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I422
Unit cell:
a: 128.928Å b: 128.928Å c: 282.825Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.228 0.284
Expression system: Escherichia coli