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1lh6
From Proteopedia
(Difference between revisions)
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<StructureSection load='1lh6' size='340' side='right'caption='[[1lh6]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1lh6' size='340' side='right'caption='[[1lh6]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1lh6]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1lh6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/European_yellow_lupin European yellow lupin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LH6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LH6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NIO:NICOTINIC+ACID'>NIO</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NIO:NICOTINIC+ACID'>NIO</scene></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=1lh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lh6 OCA], [https://pdbe.org/1lh6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lh6 RCSB], [https://www.ebi.ac.uk/pdbsum/1lh6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lh6 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/LGB2_LUPLU LGB2_LUPLU]] Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 05:54, 28 April 2021
X-RAY STRUCTURAL INVESTIGATION OF LEGHEMOGLOBIN. VI. STRUCTURE OF ACETATE-FERRILEGHEMOGLOBIN AT A RESOLUTION OF 2.0 ANGSTROMS (RUSSIAN)
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