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)
Assembly name:
PDBe Complex ID:
PDB-CPX-187314 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase SopA
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:
Sequence domains: SopA-like central domain
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%)
Sequence domains: SopA-like central domain
E3 ubiquitin-protein ligase TRIM56
Molecule details ›
Chain: B
Length: 93 amino acids
Theoretical weight: 10.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: RING-type zinc-finger
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%)
Sequence domains: RING-type zinc-finger
