7mtx

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==Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus anthracis in the complex with IMP and the inhibitor P176==
==Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus anthracis in the complex with IMP and the inhibitor P176==
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<StructureSection load='7mtx' size='340' side='right'caption='[[7mtx]]' scene=''>
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<StructureSection load='7mtx' size='340' side='right'caption='[[7mtx]], [[Resolution|resolution]] 2.44&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5urr 5urr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MTX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7mtx]] is a 8 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=5urr 5urr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MTX FirstGlance]. <br>
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</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=7mtx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mtx OCA], [https://pdbe.org/7mtx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mtx RCSB], [https://www.ebi.ac.uk/pdbsum/7mtx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mtx ProSAT]</span></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]] 2.44&#8491;</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=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZO4:N-{2-chloro-5-[({2-[3-(prop-1-en-2-yl)phenyl]propan-2-yl}carbamoyl)amino]phenyl}-beta-D-ribopyranosylamine'>ZO4</scene></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=7mtx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mtx OCA], [https://pdbe.org/7mtx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mtx RCSB], [https://www.ebi.ac.uk/pdbsum/7mtx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mtx ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A6L8P2U9_BACAN A0A6L8P2U9_BACAN] Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.[HAMAP-Rule:MF_01964]
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==See Also==
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*[[Inosine monophosphate dehydrogenase 3D structures|Inosine monophosphate dehydrogenase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus anthracis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Anderson WF]]
[[Category: Anderson WF]]

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Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus anthracis in the complex with IMP and the inhibitor P176

PDB ID 7mtx

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