5emz

X-ray diffraction
1.66Å resolution

Crystal structure of K48-linked diubiquitin with F45W mutation in the proximal unit

Released:
Source organism: Homo sapiens
Entry authors: Nakasone MA, Paukstelis PJ, Fushman D

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin Chains: A, C, E
Molecule details ›
Chains: A, C, E
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
Ubiquitin Chains: B, D, F
Molecule details ›
Chains: B, D, F
Length: 76 amino acids
Theoretical weight: 8.62 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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 58.87Å b: 78.92Å c: 91.51Å
α: 90° β: 97.93° γ: 90°
R-values:
R R work R free
0.173 0.171 0.209
Expression system: Escherichia coli