5ko7: Difference between revisions
No edit summary |
No edit summary |
||
Line 3: | Line 3: | ||
<StructureSection load='5ko7' size='340' side='right'caption='[[5ko7]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='5ko7' size='340' side='right'caption='[[5ko7]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ko7]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5ko7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Haliscomenobacter_hydrossis_DSM_1100 Haliscomenobacter hydrossis DSM 1100]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KO7 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.248Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=5ko7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ko7 OCA], [https://pdbe.org/5ko7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ko7 RCSB], [https://www.ebi.ac.uk/pdbsum/5ko7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ko7 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/IYD_HALH1 IYD_HALH1] Catalyzes the dehalogenation of halotyrosines such as 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine (PubMed:24153409, PubMed:28157283). Likely to also catalyze the dehalogenation of other halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine and 3-iodo-L-tyrosine (By similarity). Activity towards 3-iodo-L-tyrosine is much stronger than activity towards 3,5-diiodo-L-tyrosine and 2-iodophenol (PubMed:28157283, PubMed:24153409).[UniProtKB:B9K712]<ref>PMID:24153409</ref> <ref>PMID:28157283</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Line 20: | Line 21: | ||
==See Also== | ==See Also== | ||
*[[Nitroreductase|Nitroreductase]] | *[[Nitroreductase 3D structures|Nitroreductase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Haliscomenobacter hydrossis DSM 1100]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ingavat | [[Category: Ingavat N]] | ||
[[Category: Kavran | [[Category: Kavran JM]] | ||
[[Category: Rokita | [[Category: Rokita S]] | ||
[[Category: Sun | [[Category: Sun Z]] | ||