› 2wyq

X-ray diffraction
1.65Å resolution

THE CRYSTAL STRUCTURE OF THE UBIQUITIN-LIKE (UBL) DOMAIN OF HHR23A (HUMAN HOMOLOGUE A OF RAD23)

Released:
DOI: 10.2210/pdb2wyq/pdb
PDB entry 2wyq coloured by chain, front view.
PDB entry 2wyq coloured by chain, side view.
PDB entry 2wyq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structure of the ubiquitin-like (UbL) domain of human homologue A of Rad23 (hHR23A) protein.
Chen YW, Tajima T, Agrawal S
Protein Eng Des Sel 24 131-8 (2011)
PMID: 21047872

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157078 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UV excision repair protein RAD23 homolog A Chain: A
Molecule details ›
Chain: A
Length: 85 amino acids
Theoretical weight: 9.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P54725 (Residues: 1-82; Coverage: 23%)
Gene name: RAD23A
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P6522
Unit cell:
a: 78.434Å b: 78.434Å c: 63.472Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.126 0.124 0.16
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Rad23 interaction with the proteasome is regulated by phosphorylation of its ubiquitin-like (UbL) domain.
Liang et al. (2014)
2 more

2 mentions without citation

UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activity.
Guo et al. (2011)
1 more