NAD synthase

spinqualitylabelsall models NAD+ synthase complex with Mg<sup Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D +2 (green), ATP and deamino-NAD (PDB entry 1xng)' scene='54/541072/Cv/1'> Function NAD+ synthase (NADS) catalyzes the conversion of ATP, deamino-NAD+ and NH3 to AMP, NAD+ and diphosphate (PP). NADS is part of the NAD synthesis pathway . See NAD. Structural highlights The ATP binding site contains Mg+2 ion. The NAD binding site is located in the interface of the 2 subunits. Water molecules shown as red spheres.

3D Structures of NAD+ synthase

Updated on 12-August-2018

{"openlevels":0}

• NAD synthase
  • 1xng – NADS – Campylobacter jejuni
    
  • NAD – NADS (mutant) – Vibrio cholerae
    
  • 1wxf – EcNADS – Escherichia coli
    
  • 1xnh – HpNADS - Helicobacter pylori
    
  • 2pzb – BaNADS - Bacillus anthracis
    
  • 3dpi – NADS – Burkholderia pseudomallei
    
• NADS binary complex
  • 1ifx – BsNADS + deamino-NAD – Bacillus subtilis
    
  • 1wxh – EcNADS + NAD
    
  • 3hmq – BsNADS + NAD – Salmonella typhimurium
    
• NADS ternary complex
  • 1ih8 – BsNADS + Mg + ATP derivative
    
  • 1wxe – EcNADS + Mg + AMP
    
  • 1wxg – EcNADS + Mg + deamino-NAD
    
  • 2pz8 – BaNADS + Mg + ATP derivative
    
• NADS quaternary complex
  • 1ee1 – BsNADS + Mg + ATP + deamino-NAD
    
  • 1fyd – BsNADS + Mg + AMP + PP
    
  • 1kqp – BsNADS + Mg + PP + NAD derivative
    
  • 1wxi – EcNADS + Mg + AMP + PP
    
  • 1xng – HpNADS + Mg + ATP + deamino-NAD
    
  • 2pza – BaNADS + Mg + AMP + PP
    
• NADS quinary complex
  • 1nsy – BsNADS + Mg + ATP + ADP + PP
    
  • 2nsy – BsNADS + Mg + AMP + NAD + PP
    
• NADS glutamine-dependent
  • 3sdb – MtNADS (mutant) – Mycobacterium tuberculosis
    
  • 3seq, 3sez – MtNADS (mutant) + ATP derivative + pyridinium derivative
    
  • 3szg – MtNADS (mutant) + AMP + pyridinium derivative
    
  • 3syt – MtNADS + AMP + NAD + glutamate
    

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman