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1eyb
From Proteopedia
(Difference between revisions)
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<StructureSection load='1eyb' size='340' side='right'caption='[[1eyb]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1eyb' size='340' side='right'caption='[[1eyb]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1eyb]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1eyb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ey2|1ey2]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ey2|1ey2]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Homogentisate_1,2-dioxygenase Homogentisate 1,2-dioxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.5 1.13.11.5] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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> | </table> | ||
== Disease == | == 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> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 15:07, 3 November 2021
CRYSTAL STRUCTURE OF APO HUMAN HOMOGENTISATE DIOXYGENASE
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