Solution NMR

Smurf1 WW2 domain in complex with a Smad7 derived peptide


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)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase SMURF1 Chain: A
Molecule details ›
Chain: A
Length: 35 amino acids
Theoretical weight: 4.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
  • Canonical: Q9HCE7 (Residues: 306-340; Coverage: 5%)
Gene names: KIAA1625, SMURF1
Sequence domains: WW domain
Mothers against decapentaplegic homolog 7 Chain: B
Molecule details ›
Chain: B
Length: 15 amino acids
Theoretical weight: 1.78 KDa
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: O15105 (Residues: 203-217; Coverage: 4%)
Gene names: MADH7, MADH8, SMAD7

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 42%
Refinement method: torsion angle dynamics
Chemical shifts: BMR18500  
Expression systems:
  • Escherichia coli BL21
  • Not provided