Function and Biology Details
Reaction catalysed:
(1a) S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [HECT-type E3 ubiquitin transferase]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + S-ubiquitinyl-[HECT-type E3 ubiquitin transferase]-L-cysteine
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174288 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase Su(dx)
Molecule details ›
Chain: A
Length: 53 amino acids
Theoretical weight: 5.93 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: WW domain
Structure domains: Ubiquitin Ligase Nedd4; Chain: W;
Length: 53 amino acids
Theoretical weight: 5.93 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
Q9Y0H4 (Residues: 515-557; Coverage: 5%)
Sequence domains: WW domain
Structure domains: Ubiquitin Ligase Nedd4; Chain: W;
Notch C-terminal domain-containing protein
Molecule details ›
Chain: B
Length: 21 amino acids
Theoretical weight: 2.16 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli BL21
UniProt:
Length: 21 amino acids
Theoretical weight: 2.16 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli BL21
UniProt:
- Canonical: Q32UW5 (Residues: 525-540; Coverage: 2%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Refinement method:
simulated annealing
Expression system: Escherichia coli BL21
