5X3D
Crystal structure of HEP-CMP-bound form of cytidylyltransferase (CyTase) domain of Fom1 from Streptomyces wedmorensis
Summary for 5X3D
Entry DOI | 10.2210/pdb5x3d/pdb |
Descriptor | Phosphoenolpyruvate phosphomutase, [[(2R,3S,4R,5R)-5-(4-azanyl-2-oxidanylidene-pyrimidin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-(2-hydroxyethyl)phosphinic acid (3 entities in total) |
Functional Keywords | cytidylyltransferase, nucleotidyltransferase, fosfomycin biosynthesis, transferase |
Biological source | Streptomyces wedmorensis |
Total number of polymer chains | 1 |
Total formula weight | 18248.54 |
Authors | Tomita, T.,Cho, S.H.,Kuzuyama, T.,Nishiyama, M. (deposition date: 2017-02-04, release date: 2017-09-13, Last modification date: 2024-03-27) |
Primary citation | Cho, S.H.,Kim, S.Y.,Tomita, T.,Shiraishi, T.,Park, J.S.,Sato, S.,Kudo, F.,Eguchi, T.,Funa, N.,Nishiyama, M.,Kuzuyama, T. Fosfomycin Biosynthesis via Transient Cytidylylation of 2-Hydroxyethylphosphonate by the Bifunctional Fom1 Enzyme ACS Chem. Biol., 12:2209-2215, 2017 Cited by PubMed: 28727444DOI: 10.1021/acschembio.7b00419 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.93 Å) |
Structure validation
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