1odm Summary



The structure was published by Elkins, J.M., Rutledge, P.J., Burzlaff, N.I., et al., Adlington, R.M., Roach, P.L., and Baldwin, J.E., in 2003 in a paper entitled "Crystallographic Studies on the Reaction of Isopenicillin N Synthase with an Unsaturated Substrate Analogue" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.15 Å and deposited in 2003.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of ISOPENICILLIN N SYNTHASE. This molecule has the UniProt identifier P05326 (IPNS_EMENI)search. The sample contained 331 residues which is 100% of the natural sequence. Out of 331 residues 328 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A ISOPENICILLIN N SYNTHASE P05326 (1-331) (IPNS_EMENI)search Aspergillus nidulans FGSC A4search 98% 331 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P05326 (1 - 331) ISOPENICILLIN N SYNTHASE Aspergillus nidulans

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P05326) Penicillin synthase-likesearch B-lactam Antibiotic, Isopenicillin N Synthase; Chainsearch PF03171: 2OG-Fe(II) oxygenase superfamilysearch, PF14226: non-haem dioxygenase in morphine synthesis N-terminalsearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P05326) iron ion bindingsearch oxidoreductase activitysearch oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donorssearch isopenicillin-N synthase activitysearch L-ascorbic acid bindingsearch metal ion bindingsearch manganese ion bindingsearch oxidation-reduction processsearch antibiotic biosynthetic processsearch secondary metabolic processsearch penicillin biosynthetic processsearch biosynthetic processsearch cellular_componentsearch

Chain InterPro annotation
A Isopenicillin N synthase, conserved sitesearch Isopenicillin N synthasesearch Oxoglutarate/iron-dependent dioxygenasesearch Non-haem dioxygenase N-terminal domainsearch Isopenicillin N synthase-likesearch