6mgu: Difference between revisions

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<StructureSection load='6mgu' size='340' side='right'caption='[[6mgu]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
<StructureSection load='6mgu' size='340' side='right'caption='[[6mgu]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6mgu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cereus_var._anthracis"_(cohn_1872)_smith_et_al._1946 "bacillus cereus var. anthracis" (cohn 1872) smith et al. 1946]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MGU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MGU FirstGlance]. <br>
<table><tr><td colspan='2'>[[6mgu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MGU FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=JQS:5-[(Z)-(aminomethylidene)amino]-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-imidazole-4-carboxylic+acid'>JQS</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 1.54&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">guaB, BA_0008, A9486_01210, ABW01_29210, BVG01_30935, COL95_27530 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1392 "Bacillus cereus var. anthracis" (Cohn 1872) Smith et al. 1946])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=JQS:5-[(Z)-(aminomethylidene)amino]-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-imidazole-4-carboxylic+acid'>JQS</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/IMP_dehydrogenase IMP dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.205 1.1.1.205] </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=6mgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mgu OCA], [https://pdbe.org/6mgu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mgu RCSB], [https://www.ebi.ac.uk/pdbsum/6mgu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mgu 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=6mgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mgu OCA], [http://pdbe.org/6mgu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mgu RCSB], [http://www.ebi.ac.uk/pdbsum/6mgu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mgu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/A0A0J1HJU0_BACAN A0A0J1HJU0_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]  
[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]


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: IMP dehydrogenase]]
[[Category: Bacillus anthracis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Structural genomic]]
[[Category: Hedstrom L]]
[[Category: Hedstrom, L]]
[[Category: Joachimiak A]]
[[Category: Joachimiak, A]]
[[Category: Kim Y]]
[[Category: Kim, Y]]
[[Category: Maltseva N]]
[[Category: Maltseva, N]]
[[Category: Yu R]]
[[Category: Yu, R]]
[[Category: Csgid]]
[[Category: Delta cb]]
[[Category: Impdh]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]
[[Category: Tim barrel]]

Latest revision as of 09:56, 25 December 2024

Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus Anthracis in the complex with inhibitor Oxanosine monophosphate

6mgu, resolution 1.54Å

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