8ue1: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: '''Unreleased structure''' The entry 8ue1 is ON HOLD Authors: Description: Category: Unreleased Structures
 
OCA (talk | contribs)
No edit summary
 
(2 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 8ue1 is ON HOLD
==Crystal Structure of Human Fructosamine-3-kinase (FN3K)==
 
<StructureSection load='8ue1' size='340' side='right'caption='[[8ue1]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[8ue1]] 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=8UE1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8UE1 FirstGlance]. <br>
Description:  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</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=8ue1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ue1 OCA], [https://pdbe.org/8ue1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ue1 RCSB], [https://www.ebi.ac.uk/pdbsum/8ue1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ue1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FN3K_HUMAN FN3K_HUMAN] Fructosamine-3-kinase involved in protein deglycation by mediating phosphorylation of fructoselysine residues on glycated proteins, to generate fructoselysine-3 phosphate (PubMed:11016445, PubMed:11522682, PubMed:11975663). Fructoselysine-3 phosphate adducts are unstable and decompose under physiological conditions (PubMed:11522682, PubMed:11975663). Involved in intracellular deglycation in erythrocytes (PubMed:11975663). Involved in the response to oxidative stress by mediating deglycation of NFE2L2/NRF2, glycation impairing NFE2L2/NRF2 function (By similarity). Also able to phosphorylate psicosamines and ribulosamines (PubMed:14633848).[UniProtKB:Q9ER35]<ref>PMID:11016445</ref> <ref>PMID:11522682</ref> <ref>PMID:11975663</ref> <ref>PMID:14633848</ref>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Binning JM]]
[[Category: Lokhandwala J]]
[[Category: Matlack JK]]
[[Category: Miner RE]]
[[Category: Smalley TB]]
[[Category: Tran TH]]