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:
hetero dimer (preferred)
Assembly name:
E3 ubiquitin-protein ligase CBL-B and Ubiquitin (preferred)
PDBe Complex ID:
PDB-CPX-143486 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase CBL-B
Molecule details ›
Chain: A
Length: 52 amino acids
Theoretical weight: 5.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Structure domains: DNA helicase RuvA subunit, C-terminal domain
Length: 52 amino acids
Theoretical weight: 5.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
Q13191 (Residues: 924-973; Coverage: 5%)
Structure domains: DNA helicase RuvA subunit, C-terminal domain
Ubiquitin
Molecule details ›
Chain: B
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Bos taurus
UniProt:
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Bos taurus
UniProt:
- Canonical: P0CH28 (Residues: 609-684; Coverage: 11%)
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU
Spacegroup:
I222
Expression system: Escherichia coli BL21
