26xc: Difference between revisions
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The entry | ==Identification of AMPD2 Allosteric Inhibitors with Novel Mechanism of Action by Fragment Merging Approach== | ||
<StructureSection load='26xc' size='340' side='right'caption='[[26xc]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[26xc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=26XC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=26XC 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]] 2.5Å</td></tr> | |||
[[Category: | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ES9:5-CHLORO-1H-BENZIMIDAZOLE'>ES9</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=26xc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=26xc OCA], [https://pdbe.org/26xc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=26xc RCSB], [https://www.ebi.ac.uk/pdbsum/26xc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=26xc ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/AMPD2_HUMAN AMPD2_HUMAN] Autosomal recessive spastic paraplegia type 63;Pontocerebellar hypoplasia type 9. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AMPD2_HUMAN AMPD2_HUMAN] AMP deaminase plays a critical role in energy metabolism. Catalyzes the deamination of AMP to IMP and plays an important role in the purine nucleotide cycle.<ref>PMID:23911318</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Adachi T]] | |||
[[Category: Nomura A]] | |||
Latest revision as of 07:03, 17 June 2026
Identification of AMPD2 Allosteric Inhibitors with Novel Mechanism of Action by Fragment Merging Approach
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