4s2u: Difference between revisions

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==Crystal structure of the Phosphorybosylpyrophosphate synthetase from E. Coli==
==Crystal structure of the Phosphorybosylpyrophosphate synthetase from E. Coli==
<StructureSection load='4s2u' size='340' side='right' caption='[[4s2u]], [[Resolution|resolution]] 2.71&Aring;' scene=''>
<StructureSection load='4s2u' size='340' side='right'caption='[[4s2u]], [[Resolution|resolution]] 2.71&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4s2u]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S2U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4S2U FirstGlance]. <br>
<table><tr><td colspan='2'>[[4s2u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S2U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4S2U FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.71&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribose-phosphate_diphosphokinase Ribose-phosphate diphosphokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.6.1 2.7.6.1] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4s2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s2u OCA], [http://pdbe.org/4s2u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4s2u RCSB], [http://www.ebi.ac.uk/pdbsum/4s2u PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4s2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s2u OCA], [https://pdbe.org/4s2u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4s2u RCSB], [https://www.ebi.ac.uk/pdbsum/4s2u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4s2u ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KPRS_ECOLI KPRS_ECOLI] Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).[HAMAP-Rule:MF_00583]<ref>PMID:10954724</ref> <ref>PMID:2542328</ref> <ref>PMID:3009477</ref> <ref>PMID:6290219</ref> <ref>PMID:7657655</ref> <ref>PMID:8679571</ref> <ref>PMID:9125530</ref>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ribose-phosphate diphosphokinase]]
[[Category: Escherichia coli]]
[[Category: Abramchik, Y A]]
[[Category: Large Structures]]
[[Category: Esipov, R S]]
[[Category: Abramchik YA]]
[[Category: Iaroslavtceva, A K]]
[[Category: Esipov RS]]
[[Category: Kuranova, I P]]
[[Category: Iaroslavtceva AK]]
[[Category: Muravieva, T I]]
[[Category: Kuranova IP]]
[[Category: Stepanenko, V N]]
[[Category: Muravieva TI]]
[[Category: Timofeev, V I]]
[[Category: Stepanenko VN]]
[[Category: Zhukhlistova, N E]]
[[Category: Timofeev VI]]
[[Category: Atp binding]]
[[Category: Zhukhlistova NE]]
[[Category: Synthetase]]
[[Category: Transferase]]
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