X-ray diffraction
1.5Å resolution

X-ray crystal structure of the K33S mutant of ubiquitin

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 (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Ubiquitin Chains: A, B
Molecule details ›
Chains: A, B
Length: 76 amino acids
Theoretical weight: 8.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P62987 (Residues: 1-76; 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: P1
Unit cell:
a: 27.35Å b: 32.74Å c: 40.34Å
α: 69.77° β: 72.55° γ: 73.12°
R R work R free
0.168 0.165 0.19
Expression system: Escherichia coli