5qqz

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<StructureSection load='5qqz' size='340' side='right'caption='[[5qqz]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
<StructureSection load='5qqz' size='340' side='right'caption='[[5qqz]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5qqz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5QQZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5QQZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5qqz]] 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=5QQZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5QQZ 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=NUJ:trans-3-[(2,6-dimethylpyrimidin-4-yl)(methyl)amino]cyclobutan-1-ol'>NUJ</scene>, <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]] 1.55&#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=NUJ:trans-3-[(2,6-dimethylpyrimidin-4-yl)(methyl)amino]cyclobutan-1-ol'>NUJ</scene>, <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=5qqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5qqz OCA], [http://pdbe.org/5qqz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5qqz RCSB], [http://www.ebi.ac.uk/pdbsum/5qqz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5qqz 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=5qqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5qqz OCA], [https://pdbe.org/5qqz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5qqz RCSB], [https://www.ebi.ac.uk/pdbsum/5qqz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5qqz 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

PanDDA analysis group deposition -- Crystal Structure of human ALAS2A in complex with Z1675346324

PDB ID 5qqz

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