3pt3

X-ray diffraction
1.97Å resolution

Crystal structure of the C-terminal lobe of the human UBR5 HECT domain

Released:
Source organism: Homo sapiens
Primary publication:
Structure of the HECT C-lobe of the UBR5 E3 ubiquitin ligase.
Acta Crystallogr Sect F Struct Biol Cryst Commun 68 1158-63 (2012)
PMID: 23027739

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-131816 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase UBR5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 118 amino acids
Theoretical weight: 13.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O95071 (Residues: 2687-2799; Coverage: 4%)
Gene names: EDD, EDD1, HYD, KIAA0896, UBR5
Sequence domains: HECT-domain (ubiquitin-transferase)
Structure domains: Hect, E3 ligase catalytic domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P1
Unit cell:
a: 29.24Å b: 39.07Å c: 44.17Å
α: 90.04° β: 84.59° γ: 81.77°
R-values:
R R work R free
0.222 0.219 0.276
Expression system: Escherichia coli