PDBsum entry 2jb4

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Oxidoreductase PDB id
Protein chain
329 a.a. *
SO4 ×2
Waters ×403
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: Isopenicillin n synthase with a 2-thiabicycloheptan-6-one product analogue
Structure: Isopenicillin n synthetase. Chain: a. Synonym: ipns, isopenicillin n synthase. Engineered: yes
Source: Emericella nidulans. Organism_taxid: 162425. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.30Å     R-factor:   0.154     R-free:   0.176
Authors: A.C.Stewart,I.J.Clifton,R.M.Adlington,J.E.Baldwin, P.J.Rutledge
Key ref: A.C.Stewart et al. (2007). A cyclobutanone analogue mimics penicillin in binding to isopenicillin N synthase. Chembiochem, 8, 2003-2007. PubMed id: 17907118 DOI: 10.1002/cbic.200700176
01-Dec-06     Release date:   16-Oct-07    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P05326  (IPNS_EMENI) -  Isopenicillin N synthase
331 a.a.
329 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Isopenicillin-N synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Penicillin N and Deacetoxycephalosporin C Biosynthesis
      Reaction: N-((5S)-5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + O2 = isopenicillin N + 2 H2O
+ O(2)
isopenicillin N
Bound ligand (Het Group name = A14)
matches with 92.00% similarity
+ 2 × H(2)O
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cellular_component   1 term 
  Biological process     biosynthetic process   5 terms 
  Biochemical function     oxidoreductase activity     7 terms  


    Added reference    
DOI no: 10.1002/cbic.200700176 Chembiochem 8:2003-2007 (2007)
PubMed id: 17907118  
A cyclobutanone analogue mimics penicillin in binding to isopenicillin N synthase.
A.C.Stewart, I.J.Clifton, R.M.Adlington, J.E.Baldwin, P.J.Rutledge.
A carbocyclic analogue of the beta-lactam antibiotic isopenicillin N (IPN) has been synthesised and cocrystallised with isopenicillin N synthase (IPNS), the central enzyme in the biosynthesis of penicillin antibiotics. The crystal structure of the IPNS-cyclobutanone complex reveals an active site environment similar to that seen in the enzyme-product complex generated by turnover of the natural substrate within the crystalline protein. The IPNS-cyclobutanone structure demonstrates that the product analogue is tethered to the protein by hydrogen bonding and salt bridge interactions with its carboxylate groups, as seen previously for the natural substrate and product. Furthermore, the successful cocrystallisation of this analogue with IPNS provides firm structural evidence for the utility of such cyclobutanone derivatives as hydrolytically stable analogues of bicyclic beta-lactams.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19598184 W.Ge, I.J.Clifton, A.R.Howard-Jones, J.E.Stok, R.M.Adlington, J.E.Baldwin, and P.J.Rutledge (2009).
Structural studies on the reaction of isopenicillin N synthase with a sterically demanding depsipeptide substrate analogue.
  Chembiochem, 10, 2025-2031.
PDB code: 2vcm
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