› 1tbe

X-ray diffraction
2.4Å resolution

STRUCTURE OF TETRAUBIQUITIN SHOWS HOW MULTIUBIQUITIN CHAINS CAN BE FORMED

Released:
DOI: 10.2210/pdb1tbe/pdb
PDB entry 1tbe coloured by chain, front view.
PDB entry 1tbe coloured by chain, side view.
PDB entry 1tbe coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of tetraubiquitin shows how multiubiquitin chains can be formed.
Cook WJ, Jeffrey LC, Kasperek E, Pickart CM
J Mol Biol 236 601-9 (1994)
PMID: 8107144

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143418 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin Chains: A, B
Molecule details ›
Chains: A, B
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P0CG48 (Residues: 609-684; Coverage: 11%)
Gene name: UBC
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 24.1Å b: 57Å c: 47Å
α: 90° β: 94.06° γ: 90°
R-values:
R R work R free
0.184 0.184 not available
Expression system: Not provided

Quick links

Citations

16 review citations

The 26S proteasome: a molecular machine designed for controlled proteolysis.
Voges et al. (1999)
15 more

21 mentions without citation

Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.
Krishnamurthy et al. (2008)
20 more