Function and Biology Details
Reaction catalysed:
(1a) [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [RBR-type E3 ubiquitin transferase]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [RBR-type E3 ubiquitin transferase]-S-ubiquitinyl-L-cysteine
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-143413 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin
Molecule details ›
Chains: A, D
Length: 152 amino acids
Theoretical weight: 17.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Length: 152 amino acids
Theoretical weight: 17.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P0CG48 (Residues: 533-684; Coverage: 22%)
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
RanBP-type and C3HC4-type zinc finger-containing protein 1
Molecule details ›
Chains: B, E
Length: 64 amino acids
Theoretical weight: 7.28 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
Structure domains: Zn-finger domain of Sec23/24
Length: 64 amino acids
Theoretical weight: 7.28 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
- Canonical: Q9WUB0 (Residues: 192-250; Coverage: 12%)
Structure domains: Zn-finger domain of Sec23/24
