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 analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127292 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase SMURF2
Molecule details ›
Chain: A
Length: 37 amino acids
Theoretical weight: 4.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: WW domain
Length: 37 amino acids
Theoretical weight: 4.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
Q9HAU4 (Residues: 297-333; Coverage: 5%)
Sequence domains: WW domain
Mothers against decapentaplegic homolog 7
Molecule details ›
Chain: B
Length: 15 amino acids
Theoretical weight: 1.78 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
Length: 15 amino acids
Theoretical weight: 1.78 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
- Canonical: O15105 (Residues: 203-217; Coverage: 4%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
42%
Refinement method:
torsion angle dynamics
Expression systems:
- Escherichia coli BL21
- Not provided
