X-ray diffraction
1.8Å resolution

Crystal structure of the C2 Domain of the E3 Ubiquitin-Protein Ligase NEDD4

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

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
E3 ubiquitin-protein ligase NEDD4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 153 amino acids
Theoretical weight: 17.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P46934 (Residues: 517-571; Coverage: 4%)
  • Best match: P46934-4 (Residues: 1-152)
Gene names: KIAA0093, NEDD4, NEDD4-1, PIG53
Structure domains: C2 domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P1
Unit cell:
a: 38.778Å b: 47.997Å c: 50.786Å
α: 108.89° β: 111.11° γ: 100.86°
R R work R free
0.171 0.169 0.209
Expression system: Escherichia coli BL21(DE3)