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==Crystal Structure of Inosine 5'-monophosphate Dehydrogenase from Clostridium perfringens Complexed with IMP and P221== | |||
<StructureSection load='5uzc' size='340' side='right'caption='[[5uzc]], [[Resolution|resolution]] 1.85Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5uzc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens_ATCC_13124 Clostridium perfringens ATCC 13124]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UZC 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]] 1.85Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8N1:N-{2-CHLORO-5-[({2-[3-(PROP-1-EN-2-YL)PHENYL]PROPAN-2-YL}CARBAMOYL)AMINO]PHENYL}-BETA-D-XYLOFURANOSYLAMINE'>8N1</scene>, <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</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=5uzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uzc OCA], [https://pdbe.org/5uzc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uzc RCSB], [https://www.ebi.ac.uk/pdbsum/5uzc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uzc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0H2YRZ7_CLOP1 A0A0H2YRZ7_CLOP1] 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== | |||
*[[Inosine monophosphate dehydrogenase 3D structures|Inosine monophosphate dehydrogenase 3D structures]] | |||
__TOC__ | |||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Clostridium perfringens ATCC 13124]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Anderson WF]] | ||
[[Category: | [[Category: Gollapalli DR]] | ||
[[Category: | [[Category: Gu M]] | ||
[[Category: | [[Category: Hedstrom L]] | ||
[[Category: | [[Category: Joachimiak A]] | ||
[[Category: | [[Category: Kim Y]] | ||
[[Category: | [[Category: Makowska-Grzyska M]] | ||
[[Category: | [[Category: Maltseva N]] | ||
[[Category: Mulligan R]] | |||
Latest revision as of 16:37, 4 October 2023
Crystal Structure of Inosine 5'-monophosphate Dehydrogenase from Clostridium perfringens Complexed with IMP and P221Crystal Structure of Inosine 5'-monophosphate Dehydrogenase from Clostridium perfringens Complexed with IMP and P221
Structural highlights
FunctionA0A0H2YRZ7_CLOP1 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 |
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