1ey2
From Proteopedia
(Difference between revisions)
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<StructureSection load='1ey2' size='340' side='right'caption='[[1ey2]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1ey2' size='340' side='right'caption='[[1ey2]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1ey2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EY2 OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[1ey2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EY2 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></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='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">[[1eyb|1eyb]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1eyb|1eyb]]</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=1ey2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ey2 OCA], [https://pdbe.org/1ey2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ey2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ey2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ey2 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 07:16, 17 March 2021
HUMAN HOMOGENTISATE DIOXYGENASE WITH FE(II)
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