4rv4: Difference between revisions
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==2.65 Angstrom Resolution Crystal Structure of an orotate phosphoribosyltransferase from Bacillus anthracis str. 'Ames Ancestor' in complex with 5-phospho-alpha-D-ribosyl diphosphate (PRPP)== | ==2.65 Angstrom Resolution Crystal Structure of an orotate phosphoribosyltransferase from Bacillus anthracis str. 'Ames Ancestor' in complex with 5-phospho-alpha-D-ribosyl diphosphate (PRPP)== | ||
<StructureSection load='4rv4' size='340' side='right' caption='[[4rv4]], [[Resolution|resolution]] 2.65Å' scene=''> | <StructureSection load='4rv4' size='340' side='right'caption='[[4rv4]], [[Resolution|resolution]] 2.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4rv4]] is a 3 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3osc 3osc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RV4 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4rv4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3osc 3osc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RV4 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]] 2.65Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PRP:ALPHA-PHOSPHORIBOSYLPYROPHOSPHORIC+ACID'>PRP</scene></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=4rv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rv4 OCA], [https://pdbe.org/4rv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rv4 RCSB], [https://www.ebi.ac.uk/pdbsum/4rv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rv4 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/PYRE_BACAN PYRE_BACAN] Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP) (By similarity). | ||
==See Also== | ==See Also== | ||
*[[Phosphoribosyltransferase|Phosphoribosyltransferase]] | *[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus anthracis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Anderson WF]] | ||
[[Category: Halavaty | [[Category: Halavaty AS]] | ||
[[Category: Minasov | [[Category: Minasov G]] | ||
[[Category: Shuvalova | [[Category: Shuvalova L]] | ||
[[Category: Winsor | [[Category: Winsor J]] | ||
Latest revision as of 20:56, 20 September 2023
2.65 Angstrom Resolution Crystal Structure of an orotate phosphoribosyltransferase from Bacillus anthracis str. 'Ames Ancestor' in complex with 5-phospho-alpha-D-ribosyl diphosphate (PRPP)2.65 Angstrom Resolution Crystal Structure of an orotate phosphoribosyltransferase from Bacillus anthracis str. 'Ames Ancestor' in complex with 5-phospho-alpha-D-ribosyl diphosphate (PRPP)
Structural highlights
FunctionPYRE_BACAN Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP) (By similarity). See Also |
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