› 1f9j

X-ray diffraction
2.7Å resolution

STRUCTURE OF A NEW CRYSTAL FORM OF TETRAUBIQUITIN

Released:
DOI: 10.2210/pdb1f9j/pdb
PDB entry 1f9j coloured by chain, front view.
PDB entry 1f9j coloured by chain, side view.
PDB entry 1f9j coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of a new crystal form of tetraubiquitin.
Phillips CL, Thrower J, Pickart CM, Hill CP
Acta Crystallogr D Biol Crystallogr 57 341-4 (2001)
PMID: 11173499

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 tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143449 (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: Escherichia coli
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
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: I4122
Unit cell:
a: 97.02Å b: 97.02Å c: 88.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.225 0.292
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes.
Reyes-Turcu et al. (2009)
7 more

17 mentions without citation

The role of dynamic conformational ensembles in biomolecular recognition.
Boehr et al. (2009)
16 more