› 5lp8

X-ray diffraction
2.7Å resolution

Crystal structure of an asymmetric dimer of the ubiquitin ligase HUWE1

Released:
DOI: 10.2210/pdb5lp8/pdb
PDB entry 5lp8 coloured by chain, front view.
PDB entry 5lp8 coloured by chain, side view.
PDB entry 5lp8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A conformational switch regulates the ubiquitin ligase HUWE1.
Sander B, Xu W, Eilers M, Popov N, Lorenz S
Elife 6 (2017)
PMID: 28193319

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182303 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase HUWE1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 450 amino acids
Theoretical weight: 52.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7Z6Z7 (Residues: 3951-4374; Coverage: 10%)
Gene names: HSPC272, HUWE1, KIAA0312, KIAA1578, UREB1
Sequence domains: HECT-domain (ubiquitin-transferase)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE MASSIF-1
Spacegroup: P63
Unit cell:
a: 177.464Å b: 177.464Å c: 106.259Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.194 0.225
Expression system: Escherichia coli

Quick links

Citations

18 review citations

Regulating the human HECT E3 ligases.
Sluimer et al. (2018)
17 more

7 mentions without citation

A conformational switch regulates the ubiquitin ligase HUWE1.
Sander et al. (2017)
6 more