1zrr
From Proteopedia
(Difference between revisions)
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<StructureSection load='1zrr' size='340' side='right' caption='[[1zrr]], [[NMR_Ensembles_of_Models | 17 NMR models]]' scene=''> | <StructureSection load='1zrr' size='340' side='right' caption='[[1zrr]], [[NMR_Ensembles_of_Models | 17 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1zrr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1zrr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_oxytocus_perniciosus"_flugge_1886 "bacillus oxytocus perniciosus" flugge 1886]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1m4o 1m4o]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZRR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZRR FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1m4o|1m4o]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1m4o|1m4o]]</td></tr> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zrr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zrr RCSB], [http://www.ebi.ac.uk/pdbsum/1zrr PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zrr OCA], [http://pdbe.org/1zrr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zrr RCSB], [http://www.ebi.ac.uk/pdbsum/1zrr PDBsum]</span></td></tr> |
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/MTND_KLEOX MTND_KLEOX]] Catalyzes 2 different reactions between oxygene and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.<ref>PMID:8407993</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 1zrr" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bacillus oxytocus perniciosus flugge 1886]] |
[[Category: Hoefler, C]] | [[Category: Hoefler, C]] | ||
[[Category: Ju, T]] | [[Category: Ju, T]] | ||
Revision as of 04:09, 11 September 2015
Residual Dipolar Coupling Refinement of Acireductone Dioxygenase from Klebsiella
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