5qqq
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==PanDDA analysis group deposition -- Crystal Structure of human ALAS2A in complex with Z2856434857== | |
| - | + | <StructureSection load='5qqq' size='340' side='right'caption='[[5qqq]], [[Resolution|resolution]] 1.93Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5qqq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5QQQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5QQQ FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NSJ:3-[(thiomorpholin-4-yl)methyl]phenol'>NSJ</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | |
| - | [[Category: | + | <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> |
| - | [[Category: | + | <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=5qqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5qqq OCA], [http://pdbe.org/5qqq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5qqq RCSB], [http://www.ebi.ac.uk/pdbsum/5qqq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5qqq ProSAT]</span></td></tr> |
| - | [[Category: Arrowsmith, C | + | </table> |
| + | == Disease == | ||
| + | [[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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: 5-aminolevulinate synthase]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Arrowsmith, C H]] | ||
| + | [[Category: Bailey, H]] | ||
| + | [[Category: Bezerra, G A]] | ||
| + | [[Category: Bountra, C]] | ||
[[Category: Brandao-Neto, J]] | [[Category: Brandao-Neto, J]] | ||
| - | + | [[Category: Brennan, P E]] | |
| - | [[Category: Brennan, P | + | [[Category: Delft, F von]] |
| - | [[Category: | + | [[Category: Douangamath, A]] |
| - | [[Category: | + | |
[[Category: Edwards, A]] | [[Category: Edwards, A]] | ||
| - | [[Category: | + | [[Category: Foster, W]] |
| - | + | ||
[[Category: Krojer, T]] | [[Category: Krojer, T]] | ||
| - | [[Category: | + | [[Category: Nicola, B B]] |
| - | [[Category: | + | [[Category: Shrestha, L]] |
| - | [[Category: | + | [[Category: Talon, R]] |
| - | [[Category: | + | [[Category: Yue, W W]] |
| + | [[Category: Pandda]] | ||
| + | [[Category: Sgc - diamond i04-1 fragment screening]] | ||
| + | [[Category: Transferase]] | ||
| + | [[Category: Xchemexplorer]] | ||
Revision as of 05:42, 7 August 2019
PanDDA analysis group deposition -- Crystal Structure of human ALAS2A in complex with Z2856434857
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Categories: 5-aminolevulinate synthase | Large Structures | Arrowsmith, C H | Bailey, H | Bezerra, G A | Bountra, C | Brandao-Neto, J | Brennan, P E | Delft, F von | Douangamath, A | Edwards, A | Foster, W | Krojer, T | Nicola, B B | Shrestha, L | Talon, R | Yue, W W | Pandda | Sgc - diamond i04-1 fragment screening | Transferase | Xchemexplorer
