› 3egb

X-ray diffraction
3.25Å resolution

Structure of Pellino2 FHA domain at 3.3 Angstroms resolution.

Released:
DOI: 10.2210/pdb3egb/pdb
PDB entry 3egb coloured by chain, front view.
PDB entry 3egb coloured by chain, side view.
PDB entry 3egb 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

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190724 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase pellino homolog 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 285 amino acids
Theoretical weight: 31.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HAT8 (Residues: 7-289; Coverage: 67%)
Gene name: PELI2
Sequence domains: Pellino, FHA domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P212121
Unit cell:
a: 43.676Å b: 89.484Å c: 125.557Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.238 0.315
Expression system: Escherichia coli

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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

5 mentions without citation

Identification of the phosphorylation sites on the E3 ubiquitin ligase Pellino that are critical for activation by IRAK1 and IRAK4.
Smith et al. (2009)
4 more