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5X3D

Crystal structure of HEP-CMP-bound form of cytidylyltransferase (CyTase) domain of Fom1 from Streptomyces wedmorensis

Summary for 5X3D
Entry DOI10.2210/pdb5x3d/pdb
DescriptorPhosphoenolpyruvate 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 Keywordscytidylyltransferase, nucleotidyltransferase, fosfomycin biosynthesis, transferase
Biological sourceStreptomyces wedmorensis
Total number of polymer chains1
Total formula weight18248.54
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 citationCho, 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: 28727444
DOI: 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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