Function and Biology Details
Reaction catalysed:
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127207 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin/ISG15-conjugating enzyme E2 L6
Molecule details ›
Chain: A
Length: 152 amino acids
Theoretical weight: 17.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme
Length: 152 amino acids
Theoretical weight: 17.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
O14933 (Residues: 2-153; Coverage: 99%)
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme
Ubiquitin
Molecule details ›
Chain: B
Length: 76 amino acids
Theoretical weight: 8.62 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: 76 amino acids
Theoretical weight: 8.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P0CG48 (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
Chemical shift assignment:
36%
Refinement method:
torsion angle dynamics, simulated annealing
Expression system: Escherichia coli
