4gsw

X-ray diffraction
2.15Å resolution

Crystal structure of ubiquitin from Entamoeba histolytica to 2.15 Angstrom

Released:
Source organism: Entamoeba histolytica
Primary publication:
Structural determinants of ubiquitin conjugation in Entamoeba histolytica.
J Biol Chem 288 2290-302 (2013)
PMID: 23209297

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-111351 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-like domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 80 amino acids
Theoretical weight: 8.98 KDa
Source organism: Entamoeba histolytica
Expression system: Escherichia coli
UniProt:
  • Canonical: C4M760 (Residues: 1-77; Coverage: 100%)
Gene names: EHI_083270, EHI_083410, EHI_156660, EHI_178340
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P212121
Unit cell:
a: 38.631Å b: 49.865Å c: 76.824Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.193 0.256
Expression system: Escherichia coli