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==Catalytic core domain of Adenosine triphosphate phosphoribosyltransferase from Campylobacter jejuni with bound PRPP==
==Catalytic core domain of Adenosine triphosphate phosphoribosyltransferase from Campylobacter jejuni with bound PRPP==
<StructureSection load='5ubi' size='340' side='right' caption='[[5ubi]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
<StructureSection load='5ubi' size='340' side='right'caption='[[5ubi]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ubi]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UBI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UBI FirstGlance]. <br>
<table><tr><td colspan='2'>[[5ubi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni_RM1221 Campylobacter jejuni RM1221]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UBI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UBI FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PRP:ALPHA-PHOSPHORIBOSYLPYROPHOSPHORIC+ACID'>PRP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.14&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ub9|5ub9]], [[5ubg|5ubg]], [[5ubh|5ubh]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PRP:ALPHA-PHOSPHORIBOSYLPYROPHOSPHORIC+ACID'>PRP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ATP_phosphoribosyltransferase ATP phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.17 2.4.2.17] </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=5ubi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ubi OCA], [https://pdbe.org/5ubi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ubi RCSB], [https://www.ebi.ac.uk/pdbsum/5ubi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ubi ProSAT]</span></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=5ubi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ubi OCA], [http://pdbe.org/5ubi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ubi RCSB], [http://www.ebi.ac.uk/pdbsum/5ubi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ubi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/HIS1_CAMJR HIS1_CAMJR]] Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.  
[https://www.uniprot.org/uniprot/HIS1_CAMJR HIS1_CAMJR] Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5ubi" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5ubi" style="background-color:#fffaf0;"></div>
==See Also==
*[[ATP phosphoribosyl transferase 3D structures|ATP phosphoribosyl transferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: ATP phosphoribosyltransferase]]
[[Category: Campylobacter jejuni RM1221]]
[[Category: Jiao, W]]
[[Category: Large Structures]]
[[Category: Livingstone, E K]]
[[Category: Jiao W]]
[[Category: Mittelstaedt, G]]
[[Category: Livingstone EK]]
[[Category: Parker, E J]]
[[Category: Mittelstaedt G]]
[[Category: Hisg]]
[[Category: Parker EJ]]
[[Category: Histidine-biosynthesis]]
[[Category: Prpp]]
[[Category: Transferase]]
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