› 3ega

X-ray diffraction
1.8Å resolution

Crystal structure of Pellino2 FHA Domain at 1.8 Angstroms resolution

Released:
DOI: 10.2210/pdb3ega/pdb
PDB entry 3ega coloured by chain, front view.
PDB entry 3ega coloured by chain, side view.
PDB entry 3ega coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Pellino proteins contain a cryptic FHA domain that mediates interaction with phosphorylated IRAK1.
Lin CC, Huoh YS, Schmitz KR, Jensen LE, Ferguson KM
Structure 16 1806-16 (2008)
PMID: 19081057

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-190724 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase pellino homolog 2 Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 29.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HAT8 (Residues: 15-275; Coverage: 62%)
Gene name: PELI2
Sequence domains: Pellino, FHA domain

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
1 modified residue:
Ligand MSE 5 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: F222
Unit cell:
a: 83.65Å b: 86.137Å c: 162.767Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.21 0.244
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Recent insights into the structure of Toll-like receptors and post-translational modifications of their associated signalling proteins.
Carpenter et al. (2009)
8 more

6 mentions without citation

Pellino proteins contain a cryptic FHA domain that mediates interaction with phosphorylated IRAK1.
Lin et al. (2008)
5 more