1nd7

X-ray diffraction
2.1Å resolution

Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1 HECT domain E3 Ligase

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
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-190482 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NEDD4-like E3 ubiquitin-protein ligase WWP1 Chain: A
Molecule details ›
Chain: A
Length: 374 amino acids
Theoretical weight: 44.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9H0M0 (Residues: 546-917; Coverage: 40%)
Gene name: WWP1
Sequence domains: HECT-domain (ubiquitin-transferase)
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P1
Unit cell:
a: 45.2Å b: 50.85Å c: 58.43Å
α: 113.47° β: 99.21° γ: 102.26°
R-values:
R R work R free
0.243 0.243 0.27
Expression system: Escherichia coli BL21(DE3)