› 4y1h

X-ray diffraction
1.4Å resolution

Crystal structure of K33 linked tri-Ubiquitin

Released:
DOI: 10.2210/pdb4y1h/pdb
PDB entry 4y1h coloured by chain, front view.
PDB entry 4y1h coloured by chain, side view.
PDB entry 4y1h coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Assembly and structure of Lys33-linked polyubiquitin reveals distinct conformations.
Kristariyanto YA, Choi SY, Rehman SA, Ritorto MS, Campbell DG, Morrice NA, Toth R, Kulathu Y
Biochem J 467 345-52 (2015)
PMID: 25723849

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158849 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin Chain: A
Molecule details ›
Chain: A
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P62992 (Residues: 1-76; Coverage: 49%)
Gene names: RPS27A, UBA80, UBCEP1
Sequence domains: Ubiquitin family

Ligands and Environments

1 bound ligand:
Ligand EDO 4 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 28.938Å b: 41.831Å c: 47.602Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.158 0.194

Quick links

Citations

14 review citations

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

1 mention without citation

Assembly and structure of Lys33-linked polyubiquitin reveals distinct conformations.
Kristariyanto et al. (2015)