6hrh

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m (Protected "6hrh" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6hrh is ON HOLD
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==Structure of human erythroid-specific 5'-aminolevulinate synthase, ALAS2==
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<StructureSection load='6hrh' size='340' side='right' caption='[[6hrh]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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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)
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6hrh]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HRH FirstGlance]. <br>
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Description: Structure of human erythroid-specific 5'-aminolevulinate synthase, ALAS2
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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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[[Category: Unreleased Structures]]
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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='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=6hrh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hrh OCA], [http://pdbe.org/6hrh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hrh RCSB], [http://www.ebi.ac.uk/pdbsum/6hrh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hrh ProSAT]</span></td></tr>
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</table>
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== 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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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: 5-aminolevulinate synthase]]
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[[Category: Arrowsmith, C]]
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[[Category: Bailey, H J]]
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[[Category: Bountra, C]]
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[[Category: Burgess-Brown, N]]
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[[Category: Delft, F von]]
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[[Category: Diaz-saez, L]]
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[[Category: Edwards, A]]
[[Category: Kennedy, E]]
[[Category: Kennedy, E]]
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[[Category: Kupinska, K]]
[[Category: Newman, J]]
[[Category: Newman, J]]
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[[Category: Bailey, H.J]]
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[[Category: Rembeza, E]]
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[[Category: Burgess-Brown, N]]
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[[Category: Structural genomic]]
[[Category: Shrestha, L]]
[[Category: Shrestha, L]]
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[[Category: Structural Genomics Consortium (Sgc)]]
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[[Category: Yue, W W]]
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[[Category: Edwards, A]]
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[[Category: Erythroid-specific]]
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[[Category: Diaz-Saez, L]]
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[[Category: Mitochondrial]]
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[[Category: Yue, W.W]]
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[[Category: Oxidoreductase]]
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[[Category: Rembeza, E]]
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[[Category: Sgc]]
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[[Category: Von Delft, F]]
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[[Category: Bountra, C]]
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[[Category: Arrowsmith, C]]
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[[Category: Kupinska, K]]
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Revision as of 12:22, 7 November 2018

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

6hrh, resolution 2.30Å

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