› 5m93

X-ray diffraction
1.79Å resolution

Crystal structure of SdeA-modified ubiquitin.

Released:
DOI: 10.2210/pdb5m93/pdb
PDB entry 5m93 coloured by chain, front view.
PDB entry 5m93 coloured by chain, side view.
PDB entry 5m93 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination.
Bhogaraju S, Kalayil S, Liu Y, Bonn F, Colby T, Matic I, Dikic I
Cell 167 1636-1649.e13 (2016)
PMID: 27912065

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143231 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 80 amino acids
Theoretical weight: 8.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG47 (Residues: 152-228; Coverage: 34%)
Gene name: UBB
Sequence domains: Ubiquitin family

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand RIB 2 x RIB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P21
Unit cell:
a: 31.596Å b: 81.073Å c: 51.287Å
α: 90° β: 105.72° γ: 90°
R-values:
R R work R free
0.191 0.189 0.231
Expression system: Escherichia coli

Quick links

Citations

73 review citations

Ubiquitin Ligases: Structure, Function, and Regulation.
Zheng et al. (2017)
72 more