NEDD8

spinqualitylabelsall models Human NEDD8 complex with sulfate and Cl- (green) ions, 1ndd Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D NEDD8 is a ubiquitin-like protein in humans. It facilitates ubiquitin conjugation. It participates in the recruitment of E2 to the ubiquitin ligase complex. NEDD8 modifies the cullin subunits (CUL) of SCF ubiquitin E3 ligase. In yeast the protein is called Rub1. Cl coordination site is located between 2 monomers. Water molecules are shown as red spheres.

3D Structures of NEDD8

Updated on 17-November-2021

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• NEDD8
  • 1ndd - hNEDD8 - human
    
  • 2ko3 – hNEDD8 – NMR
    
• NEDD8+ubiquitin-activating enzyme E1
  • 3gzn – hNEDD8+hE1 regulatory and catalytic subunits
    
  • 3dbh, 3dbl, 3dbr - hNEDD8+hE1 regulatory and catalytic subunits (mutant)
    
  • 2nvu - hNEDD8+hE1 regulatory subunit+MBP/E1 catalytic subunit+UBC12
    
  • 1r4m - hNEDD8+hE1C+amyloid beta precursor protein
    
  • 1r4n - hNEDD8+hE1C+amyloid beta precursor protein+ATP
    
• NEDD8+other proteins
  • 3dqv – hNEDD8+CUL-5
    
  • 2bkr – hNEDD8+NEDP1
    
  • 1xt9 – hNEDD8+DEN1
    
  • 4f8c – hNEDD8 + cycle inhibiting factor
    
  • 4hcp – hNEDD8 + ATP/GTP binding protein
    
  • 4fbj – hNEDD8 + bacterial effector CIF
    
  • 4p5o – hNEDD8 + cullin-1 + E3 ubiquitin-protein ligase + DCN1-like protein + UBC12
    
  • 7oni – hNEDD8 + cullin-1 + E3 ubiquitin-protein ligase + ring-box protein – Cryo EM
    
  • 7b5n – hNEDD8 + cullin-1 + E3 ubiquitin-protein ligase + polyubiquitin – Cryo EM
    
  • 7b5l – hNEDD8 + cullin-1 + E3 ubiquitin-protein ligase + polyubiquitin + S-phase kinase-associated protein + CKS-1 – Cryo EM
    
  • 6ttu – hNEDD8 + cullin-1 + E3 ubiquitin-protein ligase + F-box/WD repeat containing protein + S-phase kinase-associated protein – Cryo EM
    
  • 6r7f – hNEDD8 in signalosome – Cryo EM
    
• Rub1
  • 1bt0 – Rub1 – Arabidopsis thaliana
    

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Jaime Prilusky