Function and Biology Details
Reaction catalysed:
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
E3 ubiquitin-protein ligase AMFR and Ubiquitin (preferred)
PDBe Complex ID:
PDB-CPX-143411 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin
Molecule details ›
Chain: A
Length: 76 amino acids
Theoretical weight: 8.58 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: 8.58 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
E3 ubiquitin-protein ligase AMFR
Molecule details ›
Chain: C
Length: 52 amino acids
Theoretical weight: 5.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: CUE domain
Structure domains: DNA helicase RuvA subunit, C-terminal domain
Length: 52 amino acids
Theoretical weight: 5.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q9UKV5 (Residues: 453-504; Coverage: 8%)
Sequence domains: CUE domain
Structure domains: DNA helicase RuvA subunit, C-terminal domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
42%
Refinement method:
simulated annealing
Expression system: Escherichia coli
