Glycosylasparaginase

spinqualitylabelsall models Structure of glycosylated human glycosylasparaginaseα (magenta and cyan) and β (green and yellow) subunits complex with asparagine (PDB code 2gl9). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Glycosylasparaginase or aspartylglucosaminidase (AGA) hydrolyzes a number of β-aspartyl amides including asparagine. AGA contains α and β subunits which derive from a precursor (PAGA) which is cleaved post-translationally. Disease AGA deficiency is the cause of the human lysosomal disease aspartylglycosaminuria. Structural highlights Glycosylated human glycosylasparaginase α and β subunits with asparagine. Mammalian AGA substrate is the protein-sugar bond of Asn-GlcNag. Water molecules shown as red spheres.

3D structures of glycosylasparaginase

Updated on 09-April-2023

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• AGA α+β subunits
  • Asparaginase – hAGA + Nag + β-mannose - human
    
  • 1apz – hAGA + Nag + β-mannose + Asp
    
  • 1ayy, 2gaw – EmAGA α+β subunits – Elizabethkingia meningoseptica
    
  • 5v2i, 6dey – EmAGA α+β (mutant) subunits
    
  • 2gl9 – EmAGA α+β (mutant) subunits + Nag + Asn
    
  • 4r4y – EmAGA α+β (mutant) subunits + hydroxyl-Asn
    
  • 1pgs – EmAGA α+β subunits – Flavobacterium meningoseptica
    
• AGA precursor
  • 2gac - EmPAGA (mutant)
    
  • 9gaa, 1p4k – EmPAGA (mutant)
    
  • 9gac, 9gaf, 1p4v, 3ljq – EmPAGA (mutant) + glycine
    

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