View source for 5hfy


==Backbone Modifications in the Protein GB1 Helix: beta-2-Ala24, beta-3-Lys28, beta-3-Lys31, beta-3-Asn35==
<StructureSection load='5hfy' size='340' side='right'caption='[[5hfy]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5hfy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp._'group_G' Streptococcus sp. 'group G']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HFY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HFY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=62H:(2S)-3-AMINO-2-METHYLPROPANOIC+ACID'>62H</scene>, <scene name='pdbligand=B3K:(3S)-3,7-DIAMINOHEPTANOIC+ACID'>B3K</scene>, <scene name='pdbligand=B3X:(3S)-3,5-DIAMINO-5-OXOPENTANOIC+ACID'>B3X</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=5hfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hfy OCA], [https://pdbe.org/5hfy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hfy RCSB], [https://www.ebi.ac.uk/pdbsum/5hfy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hfy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SPG2_STRSG SPG2_STRSG] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We report here the comparison of five classes of unnatural amino acid building blocks for their ability to be accommodated into an alpha-helix in a protein tertiary fold context. High-resolution structural characterization and analysis of folding thermodynamics yield new insights into the relationship between backbone composition and folding energetics in alpha-helix mimetics and suggest refined design rules for engineering the backbones of natural sequences.

Comparison of design strategies for alpha-helix backbone modification in a protein tertiary fold.,Tavenor NA, Reinert ZE, Lengyel GA, Griffith BD, Horne WS Chem Commun (Camb). 2016 Feb 25;52(19):3789-92. doi: 10.1039/c6cc00273k. PMID:26853882<ref>PMID:26853882</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5hfy" style="background-color:#fffaf0;"></div>

==See Also==
*[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
*[[Protein G|Protein G]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus sp. 'group G']]
[[Category: Griffith BD]]
[[Category: Horne WS]]
[[Category: Lengyel GA]]
[[Category: Reinert ZE]]
[[Category: Tavenor NA]]