Solution NMR

Structure of the second domain of human Nedd4L in complex with a phosphorylated pTPY motif derived from human Smad3


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 NEDD4-like Chain: A
Molecule details ›
Chain: A
Length: 35 amino acids
Theoretical weight: 4.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: Q96PU5 (Residues: 386-420; Coverage: 4%)
Gene names: KIAA0439, NEDD4L, NEDL3
Sequence domains: WW domain
Mothers against decapentaplegic homolog 3 Chain: B
Molecule details ›
Chain: B
Length: 12 amino acids
Theoretical weight: 1.34 KDa
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: P84022 (Residues: 178-189; Coverage: 3%)
Gene names: MADH3, SMAD3

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 49%
Refinement method: simulated annealing
Chemical shifts: BMR17544  
Expression systems:
  • Escherichia coli
  • Not provided