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2vpi

From Proteopedia

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Current revision (15:27, 13 December 2023) (edit) (undo)
 
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<StructureSection load='2vpi' size='340' side='right'caption='[[2vpi]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='2vpi' size='340' side='right'caption='[[2vpi]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2vpi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VPI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VPI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2vpi]] is a 2 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=2VPI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VPI FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/GMP_synthase_(glutamine-hydrolyzing) GMP synthase (glutamine-hydrolyzing)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.5.2 6.3.5.2] </span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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=2vpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vpi OCA], [https://pdbe.org/2vpi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vpi RCSB], [https://www.ebi.ac.uk/pdbsum/2vpi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vpi ProSAT]</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=2vpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vpi OCA], [https://pdbe.org/2vpi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vpi RCSB], [https://www.ebi.ac.uk/pdbsum/2vpi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vpi ProSAT]</span></td></tr>
</table>
</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/GUAA_HUMAN GUAA_HUMAN] A chromosomal aberration involving GMPS is found in acute myeloid leukemias. Translocation t(3,11)(q25,q23) with KMT2A/MLL1.
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== Function ==
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[https://www.uniprot.org/uniprot/GUAA_HUMAN GUAA_HUMAN] Catalyzes the conversion of xanthine monophosphate (XMP) to GMP in the presence of glutamine and ATP through an adenyl-XMP intermediate.<ref>PMID:8089153</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[GMP synthase|GMP synthase]]
*[[GMP synthase|GMP synthase]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Berg, S Van Der]]
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[[Category: Berglund H]]
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[[Category: Berglund, H]]
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[[Category: Busam RD]]
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[[Category: Busam, R D]]
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[[Category: Collins R]]
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[[Category: Collins, R]]
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[[Category: Dahlgren LG]]
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[[Category: Dahlgren, L G]]
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[[Category: Edwards AM]]
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[[Category: Edwards, A M]]
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[[Category: Flodin S]]
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[[Category: Flodin, S]]
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[[Category: Flores A]]
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[[Category: Flores, A]]
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[[Category: Graslund S]]
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[[Category: Graslund, S]]
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[[Category: Hammarstrom M]]
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[[Category: Hammarstrom, M]]
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[[Category: Herman MD]]
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[[Category: Herman, M D]]
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[[Category: Johansson I]]
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[[Category: Johansson, I]]
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[[Category: Kallas A]]
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[[Category: Kallas, A]]
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[[Category: Karlberg T]]
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[[Category: Karlberg, T]]
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[[Category: Kotenyova T]]
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[[Category: Kotenyova, T]]
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[[Category: Lehtio L]]
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[[Category: Lehtio, L]]
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[[Category: Moche M]]
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[[Category: Moche, M]]
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[[Category: Nilsson ME]]
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[[Category: Nilsson, M E]]
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[[Category: Nordlund P]]
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[[Category: Nordlund, P]]
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[[Category: Nyman T]]
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[[Category: Nyman, T]]
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[[Category: Persson C]]
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[[Category: Persson, C]]
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[[Category: Sagemark J]]
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[[Category: Structural genomic]]
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[[Category: Svensson L]]
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[[Category: Sagemark, J]]
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[[Category: Thorsell AG]]
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[[Category: Svensson, L]]
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[[Category: Tresaugues L]]
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[[Category: Thorsell, A G]]
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[[Category: Van Der Berg S]]
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[[Category: Tresaugues, L]]
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[[Category: Weigelt J]]
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[[Category: Weigelt, J]]
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[[Category: Welin M]]
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[[Category: Welin, M]]
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[[Category: Atp-binding]]
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[[Category: Chromosomal rearrangement]]
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[[Category: Cytoplasm]]
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[[Category: Glutaminase domain]]
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[[Category: Glutamine amidotransferase]]
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[[Category: Gmp]]
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[[Category: Gmp biosynthesis]]
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[[Category: Gmp synthetase]]
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[[Category: Guanine monophosphate synthetase]]
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[[Category: Ligase]]
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[[Category: Nucleotide-binding]]
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[[Category: Phosphoprotein]]
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[[Category: Proto-oncogene]]
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[[Category: Purine biosynthesis]]
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Current revision

Human GMP synthetase - glutaminase domain

PDB ID 2vpi

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