1eyb
From Proteopedia
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- | {{STRUCTURE_1eyb| PDB=1eyb | SCENE= }} | ||
- | ===CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE=== | ||
- | {{ABSTRACT_PUBMED_10876237}} | ||
- | == | + | ==CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE== |
- | [[http://www.uniprot.org/uniprot/HGD_HUMAN HGD_HUMAN | + | <StructureSection load='1eyb' size='340' side='right'caption='[[1eyb]], [[Resolution|resolution]] 1.90Å' scene=''> |
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1eyb]] is a 1 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=1EYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EYB 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]] 1.9Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1eyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eyb OCA], [https://pdbe.org/1eyb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eyb RCSB], [https://www.ebi.ac.uk/pdbsum/1eyb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eyb ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Disease == | ||
+ | [https://www.uniprot.org/uniprot/HGD_HUMAN HGD_HUMAN] Defects in HGD are the cause of alkaptonuria (AKU) [MIM:[https://omim.org/entry/203500 203500]. AKU is an autosomal recessive error of metabolism characterized by an increase in the level of homogentisic acid. The clinical manifestations of AKU are urine that turns dark on standing and alkalinization, black ochronotic pigmentation of cartilage and collagenous tissues, and spine arthritis.<ref>PMID:8782815</ref> <ref>PMID:9154114</ref> <ref>PMID:9529363</ref> <ref>PMID:9630082</ref> <ref>PMID:10205262</ref> <ref>PMID:10340975</ref> <ref>PMID:10482952</ref> <ref>PMID:10594001</ref> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/HGD_HUMAN HGD_HUMAN] | ||
+ | == 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/ey/1eyb_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=1eyb ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
- | == | + | ==See Also== |
- | [[ | + | *[[Dioxygenase 3D structures|Dioxygenase 3D structures]] |
- | + | == References == | |
- | == | + | <references/> |
- | + | __TOC__ | |
+ | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | + | [[Category: Mueller HA]] | |
- | [[Category: Mueller | + | [[Category: Penalva MA]] |
- | [[Category: Penalva | + | [[Category: Timm DE]] |
- | [[Category: Timm | + | [[Category: Titus GP]] |
- | [[Category: Titus | + | [[Category: De Cordoba SM]] |
- | [[Category: | + | |
- | + | ||
- | + |
Current revision
CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE
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