3wr5: Difference between revisions

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'''Unreleased structure'''
==Structural basis on the efficient CO2 reduction of acidophilic formate dehydrogenase==
 
<StructureSection load='3wr5' size='340' side='right' caption='[[3wr5]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
The entry 3wr5 is ON HOLD  until Paper Publication
== Structural highlights ==
 
<table><tr><td colspan='2'>[[3wr5]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WR5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WR5 FirstGlance]. <br>
Authors: Ha, J.M., Jeon, S.T., Yoon, H.J., Lee, H.H.
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
 
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Formate_dehydrogenase Formate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.2 1.2.1.2] </span></td></tr>
Description: Structural basis on the efficient CO2 reduction of acidophilic formate dehydrogenase
<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=3wr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wr5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wr5 RCSB], [http://www.ebi.ac.uk/pdbsum/3wr5 PDBsum]</span></td></tr>
[[Category: Unreleased Structures]]
</table>
[[Category: Jeon, S.T]]
__TOC__
[[Category: Ha, J.M]]
</StructureSection>
[[Category: Lee, H.H]]
[[Category: Formate dehydrogenase]]
[[Category: Yoon, H.J]]
[[Category: Ha, J M]]
[[Category: Jeon, S T]]
[[Category: Lee, H H]]
[[Category: Yoon, H J]]
[[Category: Oxidoreductase]]
[[Category: Rossmann fold]]

Revision as of 14:00, 25 February 2015

Structural basis on the efficient CO2 reduction of acidophilic formate dehydrogenase

3wr5, resolution 2.14Å

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