› 4s22

X-ray diffraction
2.3Å resolution

Crystal structure of K29 linked di-Ubiquitin

Released:
DOI: 10.2210/pdb4s22/pdb
PDB entry 4s22 coloured by chain, front view.
PDB entry 4s22 coloured by chain, side view.
PDB entry 4s22 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
K29-selective ubiquitin binding domain reveals structural basis of specificity and heterotypic nature of k29 polyubiquitin.
Kristariyanto YA, Abdul Rehman SA, Campbell DG, Morrice NA, Johnson C, Toth R, Kulathu Y
Mol Cell 58 83-94 (2015)
PMID: 25752573

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158937 (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: 8.58 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P63048 (Residues: 1-76; Coverage: 59%)
Gene names: UBA52, UBCEP2
Sequence domains: Ubiquitin family

Ligands and Environments

3 bound ligands:
Ligand IOD 6 x IOD
Ligand EDO 1 x EDO
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 33.45Å b: 69.245Å c: 60.055Å
α: 90° β: 90.22° γ: 90°
R-values:
R R work R free
0.201 0.198 0.246

Quick links

Citations

31 review citations

Ubiquitin modifications.
Swatek et al. (2016)
30 more

6 mentions without citation

Bacteria make surgical strikes on host ubiquitin signaling.
Franklin et al. (2021)
5 more