PDBe 2oni

X-ray diffraction
2.2Å resolution

Catalytic Domain of the Human NEDD4-like E3 Ligase

Released:
Source organism: Homo sapiens
Entry authors: Walker JR, Avvakumov GV, Xue S, Butler-Cole C, Weigelt J, Sundstrom M, Arrowsmith CH, Edwards AM, Bochkarev A, Dhe-Paganon S, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine. 
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer
homo hexamer
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase NEDD4-like Chain: A
Molecule details ›
Chain: A
Length: 392 amino acids
Theoretical weight: 47.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96PU5 (Residues: 594-967; Coverage: 38%)
Gene names: KIAA0439, NEDD4L, NEDL3
Structure domains:

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P6322
Unit cell:
a: 103.058Å b: 103.058Å c: 182.214Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.209 0.206 0.259
Expression system: Escherichia coli BL21(DE3)