X-ray diffraction
3.6Å resolution

Crystal structure of the human TRIM25 coiled-coil and PRYSPRY domains


Function and Biology Details

Reactions catalysed:
ATP + [ISG15] + [protein]-lysine = AMP + diphosphate + [protein]-N-ISGyllysine 
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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
E3 ubiquitin/ISG15 ligase TRIM25 Chains: A, B, E
Molecule details ›
Chains: A, B, E
Length: 445 amino acids
Theoretical weight: 50.29 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
  • Canonical: Q14258 (Residues: 189-630; Coverage: 70%)
Gene names: EFP, RNF147, TRIM25, ZNF147
Sequence domains: SPRY-associated domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P6122
Unit cell:
a: 89.92Å b: 89.92Å c: 827.09Å
α: 90° β: 90° γ: 120°
R R work R free
0.289 0.287 0.318
Expression system: Trichoplusia ni