1unb Summary



The structure was published by Valegard, K., Terwisscha Van Scheltinga, A.C., Dubus, A., et al., Oster, L.M., Hajdu, J., and Andersson, I., in 2004 in a paper entitled "The Structural Basis of Cephalosporin Formation in a Mononuclear Ferrous Enzyme" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.5 Å and deposited in 2003.

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

The PDB entry contains the structure of DEACETOXYCEPHALOSPORIN C SYNTHETASE. This molecule has the UniProt identifier P18548 (CEFE_STRC2)search. The sample contained 311 residues which is 100% of the natural sequence. Out of 311 residues 285 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 most likely forms homotrimers.

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 DEACETOXYCEPHALOSPORIN C SYNTHETASE P18548 (1-311) (CEFE_STRC2)search Streptomyces clavuligerus ATCC 27064search 98% 311 92%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P18548 (1 - 311) DEACETOXYCEPHALOSPORIN C SYNTHETASE Streptomyces clavuligerus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P18548) 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)
A (P18548) oxidoreductase activitysearch iron ion bindingsearch 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 L-ascorbic acid bindingsearch deacetoxycephalosporin-C synthase activitysearch oxidation-reduction processsearch biosynthetic processsearch antibiotic biosynthetic processsearch

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