1e51: Difference between revisions

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-{{STRUCTURE_1e51|  PDB=1e51  |  SCENE=  }}
-===CRYSTAL STRUCTURE OF NATIVE HUMAN ERYTHROCYTE 5-AMINOLAEVULINIC ACID DEHYDRATASE===
-{{ABSTRACT_PUBMED_012794073}}
-==Disease==
+==Crystal structure of native human erythrocyte 5-aminolaevulinic acid dehydratase==
-[[http://www.uniprot.org/uniprot/HEM2_HUMAN HEM2_HUMAN]] Defects in ALAD are the cause of acute hepatic porphyria (AHEPP) [MIM:[http://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>
+<StructureSection load='1e51' size='340' side='right'caption='[[1e51]], [[Resolution|resolution]] 2.83&Aring;' scene=''>
+== Structural highlights ==
-==Function==
+<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>
-[[http://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>
+</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>
-==About this Structure==
+<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>
-[[1e51]] is a 2 chain structure with sequence from [http://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].
+</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>
 ==See Also==
 *[[Porphobilinogen synthase|Porphobilinogen synthase]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:012897770</ref><references group="xtra"/><references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Porphobilinogen synthase]]
+[[Category: Large Structures]]
-[[Category: Cooper, J B.]]
+[[Category: Cooper JB]]
-[[Category: Mills-Davies, N L.]]
+[[Category: Mills-Davies NL]]
-[[Category: Shoolingin-Jordan, P M.]]
+[[Category: Shoolingin-Jordan PM]]
-[[Category: Thompson, D.]]
+[[Category: Thompson D]]
-[[Category: Dehydratase]]
-[[Category: Lead poisoning]]
-[[Category: Porphobilinogen synthase]]
-[[Category: Tetrapyrrole biosynthesis]]
-[[Category: Tim barrel]]