PDBe 5jw7

X-ray diffraction
2.85Å resolution

Crystal structure of SopA-Trim56 complex

Released:

Function and Biology Details

Reactions catalysed:
(1a) S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [HECT-type E3 ubiquitin transferase]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + S-ubiquitinyl-[HECT-type E3 ubiquitin transferase]-L-cysteine
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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase SopA Chain: A
Molecule details ›
Chain: A
Length: 282 amino acids
Theoretical weight: 31.22 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8ZNR3 (Residues: 163-425; Coverage: 34%)
Gene names: STM2066, sopA
Sequence domains: Pentapeptide repeats (9 copies)
E3 ubiquitin-protein ligase TRIM56 Chain: B
Molecule details ›
Chain: B
Length: 93 amino acids
Theoretical weight: 10.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BRZ2 (Residues: 1-93; Coverage: 12%)
Gene names: RNF109, TRIM56
Sequence domains: RING-type zinc-finger

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P3112
Unit cell:
a: 71.015Å b: 71.015Å c: 122.944Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.226 0.223 0.278
Expression system: Escherichia coli