5qrb: Difference between revisions

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<StructureSection load='5qrb' size='340' side='right'caption='[[5qrb]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
<StructureSection load='5qrb' size='340' side='right'caption='[[5qrb]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5qrb]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5QRB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5QRB FirstGlance]. <br>
<table><tr><td colspan='2'>[[5qrb]] 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=5QRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5QRB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NVY:1-ethyl-N-(2-fluorophenyl)piperidin-4-amine'>NVY</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72&#8491;</td></tr>
<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>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NVY:1-ethyl-N-(2-fluorophenyl)piperidin-4-amine'>NVY</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
<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=5qrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5qrb OCA], [http://pdbe.org/5qrb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5qrb RCSB], [http://www.ebi.ac.uk/pdbsum/5qrb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5qrb 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=5qrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5qrb OCA], [https://pdbe.org/5qrb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5qrb RCSB], [https://www.ebi.ac.uk/pdbsum/5qrb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5qrb ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== 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>
[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>  
== Function ==
[https://www.uniprot.org/uniprot/HEM0_HUMAN HEM0_HUMAN]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: 5-aminolevulinate synthase]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Bailey, H]]
[[Category: Bailey H]]
[[Category: Bezerra, G A]]
[[Category: Bezerra GA]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: Brandao-Neto, J]]
[[Category: Brandao-Neto J]]
[[Category: Brennan, P E]]
[[Category: Brennan PE]]
[[Category: Delft, F von]]
[[Category: Douangamath A]]
[[Category: Douangamath, A]]
[[Category: Edwards A]]
[[Category: Edwards, A]]
[[Category: Foster W]]
[[Category: Foster, W]]
[[Category: Krojer T]]
[[Category: Krojer, T]]
[[Category: Nicola BB]]
[[Category: Nicola, B B]]
[[Category: Shrestha L]]
[[Category: Shrestha, L]]
[[Category: Talon R]]
[[Category: Talon, R]]
[[Category: Yue WW]]
[[Category: Yue, W W]]
[[Category: Von Delft F]]
[[Category: Pandda]]
[[Category: Sgc - diamond i04-1 fragment screening]]
[[Category: Transferase]]
[[Category: Xchemexplorer]]

Latest revision as of 14:25, 21 February 2024

PanDDA analysis group deposition -- Crystal Structure of human ALAS2A in complex with Z2856434868PanDDA analysis group deposition -- Crystal Structure of human ALAS2A in complex with Z2856434868

Structural highlights

5qrb is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.72Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

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).[1]

Function

HEM0_HUMAN

References

  1. Ducamp S, Kannengiesser C, Touati M, Garcon L, Guerci-Bresler A, Guichard JF, Vermylen C, Dochir J, Poirel HA, Fouyssac F, Mansuy L, Leroux G, Tertian G, Girot R, Heimpel H, Matthes T, Talbi N, Deybach JC, Beaumont C, Puy H, Grandchamp B. Sideroblastic anemia: molecular analysis of the ALAS2 gene in a series of 29 probands and functional studies of 10 missense mutations. Hum Mutat. 2011 Jun;32(6):590-7. doi: 10.1002/humu.21455. Epub 2011 Feb 24. PMID:21309041 doi:http://dx.doi.org/10.1002/humu.21455

5qrb, resolution 1.72Å

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OCA