1fsl: Difference between revisions

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<StructureSection load='1fsl' size='340' side='right'caption='[[1fsl]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1fsl' size='340' side='right'caption='[[1fsl]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1fsl]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FSL FirstGlance]. <br>
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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=1fsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fsl OCA], [http://pdbe.org/1fsl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fsl RCSB], [http://www.ebi.ac.uk/pdbsum/1fsl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fsl ProSAT]</span></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'>[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 ==
[[http://www.uniprot.org/uniprot/LGBA_SOYBN LGBA_SOYBN]] Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation.  
[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]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fsl ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fsl ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Soybean 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<ref>PMID:15299933</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1fsl" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Glycine max]]
[[Category: Glycine max]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ellis, P J]]
[[Category: Ellis PJ]]
[[Category: Freeman, H C]]
[[Category: Freeman HC]]
[[Category: Guss, J M]]
[[Category: Guss JM]]
[[Category: Heme]]
[[Category: Multigene family]]
[[Category: Nitrogen fixation]]
[[Category: Oxygen transport]]
[[Category: Respiratory protein]]

Latest revision as of 10:18, 7 February 2024

FERRIC SOYBEAN LEGHEMOGLOBIN COMPLEXED WITH NICOTINATEFERRIC SOYBEAN LEGHEMOGLOBIN COMPLEXED WITH NICOTINATE

Structural highlights

1fsl is a 2 chain structure with sequence from Glycine max. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

1fsl, resolution 2.30Å

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OCA
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