› 2r2y

X-ray diffraction
1.7Å resolution

Crystal structure of the proteasomal Rpn13 PRU-domain

Released:
DOI: 10.2210/pdb2r2y/pdb
PDB entry 2r2y coloured by chain, front view.
PDB entry 2r2y coloured by chain, side view.
PDB entry 2r2y coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction.
Schreiner P, Chen X, Husnjak K, Randles L, Zhang N, Elsasser S, Finley D, Dikic I, Walters KJ, Groll M
Nature 453 548-52 (2008)
PMID: 18497827

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191633 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proteasomal ubiquitin receptor ADRM1 Chain: A
Molecule details ›
Chain: A
Length: 153 amino acids
Theoretical weight: 16.86 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9JKV1 (Residues: 2-150; Coverage: 37%)
Gene names: Adrm1, Gp110
Sequence domains: Proteasome complex subunit Rpn13, Pru domain
Structure domains: Proteasomal ubiquitin receptor Rpn13/ADRM1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P212121
Unit cell:
a: 42.428Å b: 56.223Å c: 63.242Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.214 0.23
Expression system: Escherichia coli

Quick links

Citations

72 review citations

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

11 mentions without citation

Recognition and processing of ubiquitin-protein conjugates by the proteasome.
Finley D. (2009)
10 more