6lnh: Difference between revisions

New page: '''Unreleased structure''' The entry 6lnh is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 6lnh is ON HOLD
==Crystal structure of IDO from Bacillus thuringiensis==
 
<StructureSection load='6lnh' size='340' side='right'caption='[[6lnh]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6lnh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LNH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LNH 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]] 2.34&#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=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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=6lnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lnh OCA], [https://pdbe.org/6lnh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lnh RCSB], [https://www.ebi.ac.uk/pdbsum/6lnh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lnh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IDO_BACTU IDO_BACTU] Catalyzes the hydroxylation of L-isoleucine to produce (4S)-4-hydroxy-L-isoleucine (PubMed:20665018, PubMed:19850012, PubMed:21821743). Can also catalyze the hydroxylation of L-leucine, L-norvaline, L-norleucine and L-allo-isoleucine, as well as the sulfoxidation of L-methionine, L-ethionine, S-methyl-L-cysteine, S-ethyl-L-cysteine, and S-allyl-L-cysteine (PubMed:21821743).<ref>PMID:19850012</ref> <ref>PMID:20665018</ref> <ref>PMID:21821743</ref>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus thuringiensis]]
[[Category: Large Structures]]
[[Category: Chen CC]]
[[Category: Feng Y]]
[[Category: Guo RT]]
[[Category: Huang JW]]
[[Category: Liu WD]]

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