PDBe 4pig

X-ray diffraction
1.95Å resolution

Crystal structure of the ubiquitin K11S mutant

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 tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 76 amino acids
Theoretical weight: 8.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62987 (Residues: 1-76; Coverage: 59%)
Gene names: UBA52, UBCEP2
Sequence domains: Ubiquitin family

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: P212121
Unit cell:
a: 47.7Å b: 61.82Å c: 91.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.169 0.218
Expression system: Escherichia coli