UV excision repair protein

Function UV excision repair protein (Rad23) is a yeast protein involved in nucleotide excision repair. The human homologs are hHR23A and hHR23B. hHR23A plays a role in translocating polyubiquitinated proteins to the proteasome. Structural highlights The protein contains a modular domain structure consisting of ubiquitin-like domain, ubiquitin-associated domain and XPC(xeroderma pigmentosum group C protein)-binding domain.

spinqualitylabelsall models Structure of yeast Rad23 (green) complex with Rad4 (grey) (PDB entry 2qsf) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

3D Structures of deaminase3D Structures of deaminase

Updated on 14-February-2018

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• Rad23
  • 2nbu – yRad23 UBA domain – yeast - NMR
    
  • 2qsf – yRad23 + Rad4
    
  • 2qsg, 2qsh, 4yir – yRad23 + Rad4 + DNA
    
  • 1x3w, 3esw – yRad23 XPC-binding domain + peptide:N-glycanase
    
  • 1x3z – yRad23 XPC-binding domain + peptide:N-glycanase + peptide
    
  • 2nbw – yRad23 UBA domain + RPN1 - NMR
    
  • 3m62 – yRad23 UBA domain + Ufd2
    
• Rad23 homolog hHR23 A
  • 1oqy, 1qze – hHR23A – human - NMR
    
  • 1f4i – hHR23A C-terminal domain (mutant) - NMR
    
  • 1ify – hHR23A internal UBA domain - NMR
    
  • 5xbo – hHR23A internal UBA domain + ubiquitin - NMR
    
  • 1p98, 2wyq – hHR23A UBA domain - NMR
    
  • 1p9d – hHR23A UBA domain + S5a - NMR
    
  • 1tp4 – hHR23A XPC-binding domain - NMR
    
• Rad23 homolog hHR23 B
  • 1p1a – hHR23B UBA domain - NMR
    
  • 1pve – hHR23B XPC-binding domain - NMR
    
  • 1uel – hHR23B UBA domain + S5a - NMR
    
  • 1x3w – HR23B XPC-binding domain + peptide:N-glycanase - mouse