6hrh: Difference between revisions

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New page: '''Unreleased structure''' The entry 6hrh is ON HOLD Authors: Bailey, H.J., Shrestha, L., Rembeza, E., Newman, J., Kupinska, K., Diaz-saez, L., Kennedy, E., Burgess-Brown, N., von Delft...
 
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'''Unreleased structure'''


The entry 6hrh is ON HOLD
==Structure of human erythroid-specific 5'-aminolevulinate synthase, ALAS2==
 
<StructureSection load='6hrh' size='340' side='right'caption='[[6hrh]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
Authors: Bailey, H.J., Shrestha, L., Rembeza, E., Newman, J., Kupinska, K., Diaz-saez, L., Kennedy, E., Burgess-Brown, N., von Delft, F., Arrowsmith, C., Edwards, A., Bountra, C., Yue, W.W., Structural Genomics Consortium (SGC)
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6hrh]] 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=6HRH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HRH FirstGlance]. <br>
Description: Structure of human erythroid-specific 5'-aminolevulinate synthase, ALAS2
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
[[Category: Unreleased Structures]]
<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>
[[Category: Kennedy, E]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6hrh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hrh OCA], [https://pdbe.org/6hrh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hrh RCSB], [https://www.ebi.ac.uk/pdbsum/6hrh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hrh ProSAT]</span></td></tr>
[[Category: Newman, J]]
</table>
[[Category: Bailey, H.J]]
== Disease ==
[[Category: Burgess-Brown, N]]
[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>
[[Category: Shrestha, L]]
== Function ==
[[Category: Structural Genomics Consortium (Sgc)]]
[https://www.uniprot.org/uniprot/HEM0_HUMAN HEM0_HUMAN]
[[Category: Edwards, A]]
== References ==
[[Category: Diaz-Saez, L]]
<references/>
[[Category: Yue, W.W]]
__TOC__
[[Category: Rembeza, E]]
</StructureSection>
[[Category: Von Delft, F]]
[[Category: Homo sapiens]]
[[Category: Bountra, C]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C]]
[[Category: Arrowsmith C]]
[[Category: Kupinska, K]]
[[Category: Bailey HJ]]
[[Category: Bountra C]]
[[Category: Burgess-Brown N]]
[[Category: Diaz-saez L]]
[[Category: Edwards A]]
[[Category: Kennedy E]]
[[Category: Kupinska K]]
[[Category: Newman J]]
[[Category: Rembeza E]]
[[Category: Shrestha L]]
[[Category: Yue WW]]
[[Category: Von Delft F]]

Latest revision as of 14:37, 24 January 2024

Structure of human erythroid-specific 5'-aminolevulinate synthase, ALAS2Structure of human erythroid-specific 5'-aminolevulinate synthase, ALAS2

Structural highlights

6hrh 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 2.3Å
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

6hrh, resolution 2.30Å

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OCA