1e51: Difference between revisions

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-[[Image:1e51.gif|left|200px]]<br /><applet load="1e51" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1e51, resolution 2.83&Aring;" />
-'''CRYSTAL STRUCTURE OF NATIVE HUMAN ERYTHROCYTE 5-AMINOLAEVULINIC ACID DEHYDRATASE'''<br />
-==Disease==
+==Crystal structure of native human erythrocyte 5-aminolaevulinic acid dehydratase==
-Known diseases associated with this structure: Lead poisoning, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=125270 125270]], Porphyria, acute hepatic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=125270 125270]]
+<StructureSection load='1e51' size='340' side='right'caption='[[1e51]], [[Resolution|resolution]] 2.83&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1e51]] 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=1E51 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E51 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.83&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PBG:3-[5-(AMINOMETHYL)-4-(CARBOXYMETHYL)-1H-PYRROL-3-YL]PROPANOIC+ACID'>PBG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1e51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e51 OCA], [https://pdbe.org/1e51 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e51 RCSB], [https://www.ebi.ac.uk/pdbsum/1e51 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e51 ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/HEM2_HUMAN HEM2_HUMAN] Defects in ALAD are the cause of acute hepatic porphyria (AHEPP) [MIM:[https://omim.org/entry/612740 612740]. A form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. AHP is characterized by attacks of gastrointestinal disturbances, abdominal colic, paralysis, and peripheral neuropathy. Most attacks are precipitated by drugs, alcohol, caloric deprivation, infections, or endocrine factors.<ref>PMID:1569184</ref> <ref>PMID:2063868</ref> <ref>PMID:1309003</ref> <ref>PMID:10706561</ref> <ref>PMID:17236137</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/HEM2_HUMAN HEM2_HUMAN] Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.<ref>PMID:11032836</ref> <ref>PMID:19812033</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e5/1e51_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1e51 ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-E51 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN, SO4 and PBG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Porphobilinogen_synthase Porphobilinogen synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.24 4.2.1.24] Known structural/functional Site: <scene name='pdbsite=ZN:Zn A 501 Is Bound Covalently By CYS 122, 124, 132'>ZN</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E51 OCA].
+*[[Porphobilinogen synthase|Porphobilinogen synthase]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Porphobilinogen synthase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Cooper JB]]
-[[Category: Cooper, J.B.]]
+[[Category: Mills-Davies NL]]
-[[Category: Mills-Davies, N.L.]]
+[[Category: Shoolingin-Jordan PM]]
-[[Category: Shoolingin-Jordan, P.M.]]
+[[Category: Thompson D]]
-[[Category: Thompson, D.]]
-[[Category: PBG]]
-[[Category: SO4]]
-[[Category: ZN]]
-[[Category: dehydratase]]
-[[Category: lead poisoning]]
-[[Category: porphobilinogen synthase]]
-[[Category: tetrapyrrole biosynthesis]]
-[[Category: tim barrel]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:56:55 2007''