8y59

X-ray diffraction
1.89Å resolution

Crystal structure of TRIM21 PRYSPRY (D355A) in complex with (S)-hydroxyl-acepromazine.

Released:

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-539136 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase TRIM21 Chain: A
Molecule details ›
Chain: A
Length: 192 amino acids
Theoretical weight: 21.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P19474 (Residues: 287-475; Coverage: 40%)
Gene names: RNF81, RO52, SSA1, TRIM21
Sequence domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17UM
Spacegroup: P41212
Unit cell:
a: 100.908Å b: 100.908Å c: 49.955Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.186 0.234
Expression system: Escherichia coli