Isopenicillin N synthase

spinqualitylabelsall models Isopenicilln N synthase complex with ACV and NO, 1blz Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Isopenicillin N synthase (IPNS) is an iron-dependent enzyme which catalyzes the formation of isopenicillin N (IPN) from the tripeptide aminoadipoyl-cysteine-valine (ACV). IPNS participates in the biosynthesis of penicillin and cephalosporin antibiotics. The active site of IPNS contains an Fe atom. The reaction involves the reduction of O2 molecule to H2O. Structural highlights IPNS active site contains Fe+2 and the substrate ACV. The Fe+2 ion is hexacoordinated to 3 IPNS side chains, one water molecule, the ACV thiolate moiety and NO. Water molecules shown as red spheres.

3D structures of isopenicillin N synthase

Updated on 24-June-2019

{"openlevels":0}

• Fe containing IPNS
  • 1bk0 - AnIPNS + ACV – Aspergillus nidulans
    
  • 2bjs - AnIPNS (mutant) + ACV
    
  • 1qiq, 1qjf, 1hb1, 1hb2, 1hb3, 1hb4, 1odm, 1odn, 1oc1, 1uzw, 1w03, 1w05, 2bu9, 1w3v, 1w3x, 2ivi, 2ivj, 2vau, 2vbb, 2vbd, 2vbp, 2vcm, 2ve1, 2wo7, 2y6f, 2y60, 4bb3 - AnIPNS + ACV derivative
    
  • 2jb4 - AnIPNS + cyclobutanone analog
    
  • 1qje - AnIPNS + IPN + ACV
    
  • 1blz - AnIPNS + NO + ACV
    
  • 1obn, 1w04, 1w06 - AnIPNS + hydroxylamine + ACV derivative
    
  • 3zku, 3zky, 3zoi, 4bb3 - IPNS + ACV derivative – Emericella nidulans
    
• Mn containing IPNS
  • 1ips – AnIPNS

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