› 2vok

X-ray diffraction
1.3Å resolution

Murine TRIM21

Released:
DOI: 10.2210/pdb2vok/pdb
PDB entry 2vok coloured by chain, front view.
PDB entry 2vok coloured by chain, side view.
PDB entry 2vok coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
TRIM21 is an IgG receptor that is structurally, thermodynamically, and kinetically conserved.
Keeble AH, Khan Z, Forster A, James LC
Proc Natl Acad Sci U S A 105 6045-50 (2008)
PMID: 18420815

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:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178919 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase TRIM21 Chains: A, B
Molecule details ›
Chains: A, B
Length: 188 amino acids
Theoretical weight: 21.54 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q62191 (Residues: 291-470; Coverage: 38%)
Gene names: Ro52, Ssa1, Trim21
Sequence domains:
Structure domains: Jelly Rolls

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21
Unit cell:
a: 62.955Å b: 44.889Å c: 71.794Å
α: 90° β: 109.89° γ: 90°
R-values:
R R work R free
0.215 0.214 0.236
Expression system: Escherichia coli

Quick links

Citations

43 review citations

IgG subclasses and allotypes: from structure to effector functions.
Vidarsson et al. (2014)
42 more

7 mentions without citation

Structure and function of the SPRY/B30.2 domain proteins involved in innate immunity.
D'Cruz et al. (2013)
6 more