6flm

X-ray diffraction
2.01Å resolution

Crystal structure of the human TRIM25 PRYSPRY domain

Released:

Function and Biology Details

Reactions 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
ATP + [ISG15] + [protein]-lysine = AMP + diphosphate + [protein]-N-ISGyllysine 
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin/ISG15 ligase TRIM25 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 199 amino acids
Theoretical weight: 22.7 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q14258 (Residues: 435-630; Coverage: 31%)
Gene names: EFP, RNF147, TRIM25, ZNF147
Sequence domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P321
Unit cell:
a: 152.75Å b: 152.75Å c: 68.96Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.167 0.165 0.206
Expression system: Trichoplusia ni