PDBe 4pij

X-ray diffraction
1.5Å resolution

X-ray crystal structure of the K11S/K63S double mutant of ubiquitin

Released:
Source organism: Homo sapiens
Primary publication:
Enhancing ubiquitin crystallization through surface-entropy reduction.
Acta Crystallogr F Struct Biol Commun 70 1434-42 (2014)
PMID: 25286958

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin Chains: A, B
Molecule details ›
Chains: A, B
Length: 75 amino acids
Theoretical weight: 8.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62987 (Residues: 1-75; Coverage: 59%)
Gene names: UBA52, UBCEP2
Sequence domains: Ubiquitin family

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 31.97Å b: 48.85Å c: 80.32Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.176 0.198
Expression system: Escherichia coli