5qt3

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Current revision (11:27, 21 February 2024) (edit) (undo)
 
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<StructureSection load='5qt3' size='340' side='right'caption='[[5qt3]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='5qt3' size='340' side='right'caption='[[5qt3]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5qt3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5QT3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5QT3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5qt3]] 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=5QT3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5QT3 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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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]] 1.95&#8491;</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/5-aminolevulinate_synthase 5-aminolevulinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.37 2.3.1.37] </span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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=5qt3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5qt3 OCA], [http://pdbe.org/5qt3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5qt3 RCSB], [http://www.ebi.ac.uk/pdbsum/5qt3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5qt3 ProSAT]</span></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=5qt3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5qt3 OCA], [https://pdbe.org/5qt3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5qt3 RCSB], [https://www.ebi.ac.uk/pdbsum/5qt3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5qt3 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/HEM0_HUMAN HEM0_HUMAN]] X-linked sideroblastic anemia;Erythropoietic protoporphyria. 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. Gain of function mutations in ALS2 are responsible for XLDPT, but they can also be a possible aggravating factor in congenital erythropoietic porphyria and other erythropoietic disorders caused by mutations in other genes (PubMed:21309041).<ref>PMID:21309041</ref>
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[https://www.uniprot.org/uniprot/HEM0_HUMAN HEM0_HUMAN] X-linked sideroblastic anemia;Erythropoietic protoporphyria. 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. Gain of function mutations in ALS2 are responsible for XLDPT, but they can also be a possible aggravating factor in congenital erythropoietic porphyria and other erythropoietic disorders caused by mutations in other genes (PubMed:21309041).<ref>PMID:21309041</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/HEM0_HUMAN HEM0_HUMAN]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: 5-aminolevulinate synthase]]
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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: Bailey, H]]
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[[Category: Bailey H]]
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[[Category: Bezerra, G A]]
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[[Category: Bezerra GA]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Brandao-Neto, J]]
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[[Category: Brandao-Neto J]]
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[[Category: Brennan, P E]]
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[[Category: Brennan PE]]
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[[Category: Delft, F von]]
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[[Category: Douangamath A]]
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[[Category: Douangamath, A]]
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[[Category: Edwards A]]
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[[Category: Edwards, A]]
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[[Category: Foster W]]
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[[Category: Foster, W]]
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[[Category: Krojer T]]
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[[Category: Krojer, T]]
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[[Category: Nicola BB]]
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[[Category: Nicola, B B]]
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[[Category: Shrestha L]]
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[[Category: Shrestha, L]]
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[[Category: Talon R]]
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[[Category: Talon, R]]
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[[Category: Yue WW]]
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[[Category: Yue, W W]]
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[[Category: Von Delft F]]
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[[Category: Pandda]]
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[[Category: Sgc - diamond i04-1 fragment screening]]
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[[Category: Transferase]]
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[[Category: Xchemexplorer]]
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Current revision

Ground state model of human erythroid-specific 5'-aminolevulinate synthase, ALAS2 - SGC Diamond Xchem fragment screening

PDB ID 5qt3

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