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1o64
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==Crystal structure of an ATP phosphoribosyltransferase== | ==Crystal structure of an ATP phosphoribosyltransferase== | ||
| - | <StructureSection load='1o64' size='340' side='right' caption='[[1o64]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='1o64' size='340' side='right'caption='[[1o64]], [[Resolution|resolution]] 2.10Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1o64]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1o64]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O64 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |
| - | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1o64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o64 OCA], [https://pdbe.org/1o64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o64 RCSB], [https://www.ebi.ac.uk/pdbsum/1o64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o64 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/HIS1_THEMA HIS1_THEMA] 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 (By similarity). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</div> | </div> | ||
<div class="pdbe-citations 1o64" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1o64" 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: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Thermotoga maritima]] |
| - | [[Category: GenomiX | + | [[Category: Structural GenomiX]] |
| - | + | ||
| - | + | ||
Current revision
Crystal structure of an ATP phosphoribosyltransferase
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