2qho

X-ray diffraction
1.85Å resolution

Crystal structure of the UBA domain from EDD ubiquitin ligase in complex with ubiquitin

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P0CH28 (Residues: 609-684; Coverage: 11%)
Gene name: UBC
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
E3 ubiquitin-protein ligase UBR5 Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 53 amino acids
Theoretical weight: 5.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O95071 (Residues: 180-230; Coverage: 2%)
Gene names: EDD, EDD1, HYD, KIAA0896, UBR5
Structure domains: DNA helicase RuvA subunit, C-terminal domain

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 33.849Å b: 59.333Å c: 246.672Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.258
Expression system: Escherichia coli BL21