2nsq

X-ray diffraction
1.85Å resolution

Crystal structure of the C2 domain of the human E3 ubiquitin-protein ligase NEDD4-like protein

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

Function and Biology Details

Reactions 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
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-188677 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase NEDD4-like Chain: A
Molecule details ›
Chain: A
Length: 155 amino acids
Theoretical weight: 17.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96PU5 (Residues: 1-154; Coverage: 16%)
Gene names: KIAA0439, NEDD4L, NEDL3
Sequence domains: C2 domain
Structure domains: C2 domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 32.93Å b: 60.036Å c: 74.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.171 0.218
Expression system: Escherichia coli BL21(DE3)