5o44

X-ray diffraction
3.14Å resolution

Crystal structure of unbranched mixed tri-Ubiquitin chain containing K48 and K63 linkages.

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero 12-mer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ubiquitin-like domain-containing protein Chains: A, E
Molecule details ›
Chains: A, E
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Musca domestica
Expression system: Escherichia coli
UniProt:
  • Canonical: Q45TR8 (Residues: 1-76; Coverage: 100%)
Sequence domains: Ubiquitin family
Ubiquitin Chains: B, C
Molecule details ›
Chains: B, C
Length: 74 amino acids
Theoretical weight: 8.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG47 (Residues: 153-226; Coverage: 32%)
Gene name: UBB
Sequence domains: Ubiquitin family
Ubiquitin Chains: D, F
Molecule details ›
Chains: D, F
Length: 76 amino acids
Theoretical weight: 8.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG47 (Residues: 153-228; Coverage: 33%)
Gene name: UBB
Sequence domains: Ubiquitin family

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID30B
Spacegroup: P6122
Unit cell:
a: 110.767Å b: 110.767Å c: 417.004Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.219 0.217 0.254
Expression system: Escherichia coli