› 3h1d

X-ray diffraction
1.89Å resolution

Structure of the HUWE1 HECT Domain

Released:
DOI: 10.2210/pdb3h1d/pdb
PDB entry 3h1d coloured by chain, front view.
PDB entry 3h1d coloured by chain, side view.
PDB entry 3h1d coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A structural element within the HUWE1 HECT domain modulates self-ubiquitination and substrate ubiquitination activities.
Pandya RK, Partridge JR, Love KR, Schwartz TU, Ploegh HL
J Biol Chem 285 5664-73 (2010)
PMID: 20007713

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182301 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase HUWE1 Chain: A
Molecule details ›
Chain: A
Length: 405 amino acids
Theoretical weight: 47.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7Z6Z7 (Residues: 3993-4374; Coverage: 9%)
Gene names: HSPC272, HUWE1, KIAA0312, KIAA1578, UREB1
Sequence domains: HECT-domain (ubiquitin-transferase)
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2
Unit cell:
a: 119.654Å b: 55.653Å c: 69.585Å
α: 90° β: 122.49° γ: 90°
R-values:
R R work R free
0.169 0.166 0.229
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Mammalian HECT ubiquitin-protein ligases: biological and pathophysiological aspects.
Scheffner et al. (2014)
9 more

11 mentions without citation

HECT E3 ubiquitin ligases - emerging insights into their biological roles and disease relevance.
Wang et al. (2020)
10 more