ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ANAEROBIC AC-VINYLGLYCINE FE COMPLEX)
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). 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):
This entry contains 1 unique UniProt protein: