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:
Biological process:
- not assigned
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188462 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
RanBP-type and C3HC4-type zinc finger-containing protein 1
Molecule details ›
Chain: A
Length: 105 amino acids
Theoretical weight: 11.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Length: 105 amino acids
Theoretical weight: 11.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9BYM8 (Residues: 37-137; Coverage: 20%)
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
E3 ubiquitin-protein ligase RNF31
Molecule details ›
Chain: B
Length: 162 amino acids
Theoretical weight: 18.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: HOIP UBA domain pair
Structure domains:
Length: 162 amino acids
Theoretical weight: 18.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q96EP0 (Residues: 480-636; Coverage: 15%)
Sequence domains: HOIP UBA domain pair
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SPRING-8 BEAMLINE BL44XU
Spacegroup:
P3121
Expression system: Escherichia coli
