4fo4: Difference between revisions

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New page: '''Unreleased structure''' The entry 4fo4 is ON HOLD Authors: Osipiuk, J., Maltseva, N., Makowska-Grzyska, M., Gu, M., Anderson, W.F., Joachimiak, A., Center for Structural Genomics of ...
 
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'''Unreleased structure'''


The entry 4fo4 is ON HOLD
==Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion mutant, complexed with IMP and mycophenolic acid==
<StructureSection load='4fo4' size='340' side='right'caption='[[4fo4]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4fo4]] 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=4FO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FO4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.03&#8491;</td></tr>
<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=MOA:MYCOPHENOLIC+ACID'>MOA</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=4fo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fo4 OCA], [https://pdbe.org/4fo4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fo4 RCSB], [https://www.ebi.ac.uk/pdbsum/4fo4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fo4 ProSAT]</span></td></tr>
</table>
== Function ==
[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]


Authors: Osipiuk, J., Maltseva, N., Makowska-Grzyska, M., Gu, M., Anderson, W.F., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)
==See Also==
 
*[[Inosine monophosphate dehydrogenase 3D structures|Inosine monophosphate dehydrogenase 3D structures]]
Description: Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion mutant, complexed with IMP and mycophenolic acid.
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio cholerae O1 biovar El Tor str. N16961]]
[[Category: Anderson WF]]
[[Category: Gu M]]
[[Category: Joachimiak A]]
[[Category: Makowska-Grzyska M]]
[[Category: Maltseva N]]
[[Category: Osipiuk J]]

Latest revision as of 15:30, 14 March 2024

Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion mutant, complexed with IMP and mycophenolic acid

4fo4, resolution 2.03Å

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