PDBe 2lb0

Solution NMR

Structure of the first WW domain of human Smurf1 in complex with a di-phosphorylated human Smad1 derived peptide

Released:

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: 36 amino acids
Theoretical weight: 4.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HCE7 (Residues: 235-267; Coverage: 4%)
Gene names: KIAA1625, SMURF1
Sequence domains: WW domain
Mothers against decapentaplegic homolog 1 Chain: B
Molecule details ›
Chain: B
Length: 10 amino acids
Theoretical weight: 1.18 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q15797 (Residues: 208-217; Coverage: 2%)
Gene names: BSP1, MADH1, MADR1, SMAD1

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 40%
Refinement method: simulated annealing
Chemical shifts: BMR17542  
Expression systems:
  • Escherichia coli
  • Not provided