4x3z

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==Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion mutant, in complex with XMP and NAD==
==Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion mutant, in complex with XMP and NAD==
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<StructureSection load='4x3z' size='340' side='right' caption='[[4x3z]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
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<StructureSection load='4x3z' size='340' side='right'caption='[[4x3z]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4x3z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibch Vibch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X3Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X3Z FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4x3z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_O1_biovar_El_Tor_str._N16961 Vibrio cholerae O1 biovar El Tor str. N16961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X3Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X3Z FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=XMP:XANTHOSINE-5-MONOPHOSPHATE'>XMP</scene></td></tr>
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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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=XMP:XANTHOSINE-5-MONOPHOSPHATE'>XMP</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fxs|4fxs]], [[4qne|4qne]], [[4qq3|4qq3]], [[4fo4|4fo4]], [[4ff0|4ff0]], [[4fez|4fez]]</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=4x3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x3z OCA], [https://pdbe.org/4x3z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x3z RCSB], [https://www.ebi.ac.uk/pdbsum/4x3z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x3z ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">guaB, VC_0767 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</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/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>
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<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=4x3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x3z OCA], [http://pdbe.org/4x3z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x3z RCSB], [http://www.ebi.ac.uk/pdbsum/4x3z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x3z ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/Q9KTW3_VIBCH Q9KTW3_VIBCH]] 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 (By similarity).[HAMAP-Rule:MF_01964]
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[https://www.uniprot.org/uniprot/Q9KTW3_VIBCH Q9KTW3_VIBCH] 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 (By similarity).[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: IMP dehydrogenase]]
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[[Category: Large Structures]]
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[[Category: Vibch]]
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[[Category: Vibrio cholerae O1 biovar El Tor str. N16961]]
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[[Category: Anderson, W F]]
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[[Category: Anderson WF]]
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[[Category: Structural genomic]]
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[[Category: Gu M]]
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[[Category: Gu, M]]
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[[Category: Joachimiak A]]
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[[Category: Joachimiak, A]]
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[[Category: KIM Y]]
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[[Category: KIM, Y]]
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[[Category: MAKOWSKA-GRZYSKA M]]
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[[Category: MAKOWSKA-GRZYSKA, M]]
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[[Category: MALTSEVA N]]
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[[Category: MALTSEVA, N]]
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[[Category: Mulligan R]]
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[[Category: Mulligan, R]]
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[[Category: Osipiuk J]]
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[[Category: Osipiuk, J]]
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[[Category: Csgid]]
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[[Category: Impdh]]
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[[Category: Inosine 5'-monophosphate dehydrogenase]]
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[[Category: Oxidoreductase]]
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[[Category: Xanthosine monophosphate]]
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[[Category: Xmp]]
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Revision as of 21:11, 12 April 2023

Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion mutant, in complex with XMP and NAD

PDB ID 4x3z

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