1de2
From Proteopedia
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<StructureSection load='1de2' size='340' side='right'caption='[[1de2]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | <StructureSection load='1de2' size='340' side='right'caption='[[1de2]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1de2]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1de2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DE2 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1de1|1de1]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1de1|1de1]]</div></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=1de2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1de2 OCA], [https://pdbe.org/1de2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1de2 RCSB], [https://www.ebi.ac.uk/pdbsum/1de2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1de2 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/GLRX_BPT4 GLRX_BPT4]] Serves as a reducing agent for the phage-induced ribonucleotide reductase, but not for the bacterial ones. This specificity may be the result of sequence differences around the redox-active disulfide bond. The oxidized form accepts electrons from bacterial glutathione and will, in turn, reduce other small disulfides. Can also be reduced by NADPH and by bacterial thioredoxin reductase.<ref>PMID:8440680</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 18:25, 10 March 2021
NMR STRUCTURES OF REDUCED BACTERIOPHAGE T4 GLUTAREDOXIN
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