› 2f0r

X-ray diffraction
2.26Å resolution

Crystallographic structure of human Tsg101 UEV domain

Released:
DOI: 10.2210/pdb2f0r/pdb
PDB entry 2f0r coloured by chain, front view.
PDB entry 2f0r coloured by chain, side view.
PDB entry 2f0r coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of human TSG101 UEV domain.
Palencia A, Martinez JC, Mateo PL, Luque I, Camara-Artigas A
Acta Crystallogr D Biol Crystallogr 62 458-64 (2006)
PMID: 16552148

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189274 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tumor susceptibility gene 101 protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 159 amino acids
Theoretical weight: 18.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99816 (Residues: 1-145; Coverage: 37%)
Gene name: TSG101
Sequence domains: UEV domain
Structure domains: Ubiquitin Conjugating Enzyme

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: R3
Unit cell:
a: 97.865Å b: 97.865Å c: 110.583Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.188 0.243
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Membrane protein targeting to the MVB/lysosome.
Davies et al. (2009)
1 more

4 mentions without citation

Anatomy of the E2 ligase fold: implications for enzymology and evolution of ubiquitin/Ub-like protein conjugation.
Burroughs et al. (2008)
3 more