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1o64

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Current revision (23:46, 27 December 2023) (edit) (undo)
 
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<StructureSection load='1o64' size='340' side='right'caption='[[1o64]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1o64' size='340' side='right'caption='[[1o64]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1o64]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1O64 FirstGlance]. <br>
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<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HISG, TM1042 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>
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<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>
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<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>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1o64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o64 OCA], [http://pdbe.org/1o64 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o64 RCSB], [http://www.ebi.ac.uk/pdbsum/1o64 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o64 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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).
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[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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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: ATP phosphoribosyltransferase]]
 
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[[Category: Atcc 43589]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: GenomiX, Structural]]
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[[Category: Thermotoga maritima]]
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[[Category: Structural genomic]]
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[[Category: Structural GenomiX]]
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[[Category: Transferase]]
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Current revision

Crystal structure of an ATP phosphoribosyltransferase

PDB ID 1o64

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