5x3d: Difference between revisions
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==Crystal structure of HEP-CMP-bound form of cytidylyltransferase (CyTase) domain of Fom1 from Streptomyces wedmorensis== | |||
<StructureSection load='5x3d' size='340' side='right'caption='[[5x3d]], [[Resolution|resolution]] 1.93Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5x3d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_wedmorensis Streptomyces wedmorensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X3D FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.93Å</td></tr> | |||
[[Category: | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7XL:[[(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'>7XL</scene></td></tr> | ||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5x3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x3d OCA], [https://pdbe.org/5x3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x3d RCSB], [https://www.ebi.ac.uk/pdbsum/5x3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x3d ProSAT]</span></td></tr> | ||
[[Category: | </table> | ||
[[Category: Kuzuyama | == Function == | ||
[[Category: | [https://www.uniprot.org/uniprot/FOM1_STRWE FOM1_STRWE] Bifunctional enzyme that catalyzes two steps during fosfomycin biosynthesis (PubMed:28727444). It catalyzes the conversion of phosphoenolpyruvate (PEP) to phosphonopyruvate (PnPy), the first step of the pathway. It also catalyzes the cytidylylation of the 2-hydroxyethylphosphonate (HEP) intermediate to produce cytidylyl-2-hydroxyethylphosphonate (HEP-CMP), the fourth step of the pathway (PubMed:28727444).<ref>PMID:28727444</ref> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces wedmorensis]] | |||
[[Category: Cho SH]] | |||
[[Category: Kuzuyama T]] | |||
[[Category: Nishiyama M]] | |||
[[Category: Tomita T]] | |||
Latest revision as of 10:17, 27 March 2024
Crystal structure of HEP-CMP-bound form of cytidylyltransferase (CyTase) domain of Fom1 from Streptomyces wedmorensis
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