1fsl: Difference between revisions
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<StructureSection load='1fsl' size='340' side='right'caption='[[1fsl]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1fsl' size='340' side='right'caption='[[1fsl]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fsl]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1fsl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FSL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FSL 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=1fsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fsl OCA], [https://pdbe.org/1fsl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fsl RCSB], [https://www.ebi.ac.uk/pdbsum/1fsl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fsl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/LGBA_SOYBN LGBA_SOYBN]] 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 19:11, 27 October 2021
FERRIC SOYBEAN LEGHEMOGLOBIN COMPLEXED WITH NICOTINATEFERRIC SOYBEAN LEGHEMOGLOBIN COMPLEXED WITH NICOTINATE
Structural highlights
Function[LGBA_SOYBN] Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSoybean leghemoglobin a is a small (16 kDa) protein facilitating the transport of O(2) to respiring N(2)-fixing bacteria at low free-O(2) tension. The crystal structure of soybean ferric leghemoglobin a nicotinate has been refined at 2.3 A resolution. The final R factor is 15.8% for 6877 reflections between 6.0 and 2.3 A. The structure of soybean leghemoglobin a (143 residues) is closely similar to that of lupin leghemoglobin II (153 residues), the proteins having 82 identical residues when the sequences are aligned. The new structure provides support for the conclusion that the unique properties of leghemoglobin arise principally from a heme pocket considerably larger and more flexible than that of myoglobin, a strongly ruffled heme group, and a proximal histidine orientation more favourable to ligand binding. Structure of ferric soybean leghemoglobin a nicotinate at 2.3 A resolution.,Ellis PJ, Appleby CA, Guss JM, Hunter WN, Ollis DL, Freeman HC Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):302-10. PMID:15299933[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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