› 3efu

X-ray diffraction
1.84Å resolution

X-ray structure of human ubiquitin-Hg(II) adduct

Released:
DOI: 10.2210/pdb3efu/pdb
PDB entry 3efu coloured by chain, front view.
PDB entry 3efu coloured by chain, side view.
PDB entry 3efu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural probing of Zn(II), Cd(II) and Hg(II) binding to human ubiquitin.
Falini G, Fermani S, Tosi G, Arnesano F, Natile G
Chem Commun (Camb) 5960-2 (2008)
PMID: 19030552

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143327 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin Chain: A
Molecule details ›
Chain: A
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG48 (Residues: 609-684; Coverage: 11%)
Gene name: UBC
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

1 bound ligand:
Ligand HG 1 x HG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P212121
Unit cell:
a: 28.024Å b: 42.828Å c: 50.374Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.235 0.293
Expression system: Escherichia coli

Quick links

Citations

17 citation in other articles

TDP-43 N terminus encodes a novel ubiquitin-like fold and its unfolded form in equilibrium that can be shifted by binding to ssDNA.
Qin et al. (2014)
16 more

2 mentions without citation

Dynamics may significantly influence the estimation of interatomic distances in biomolecular X-ray structures.
Kuzmanic et al. (2011)
1 more