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<head><link rel = 'stylesheet' href = 'style.css'><script src='https://3Dmol.org/build/3Dmol-min.js'></script><title>ReDisulphID</title></head><body><div class= 'title'>ReDisulphID<div class='subtitle'><p>a tool for identifying redox-active intermolecular disulphides from structures</div></div><div class = 'main'><div class = 'item structure' style='background:;'><p class = 'struc' hidden>1b2d A 11 B 7</p><div style='height: 100%; position: relative;' class='viewer_3Dmoljs' id='viewer' data-pdb='1b2d' data-backgroundcolor='0xffffff' data-surface='opacity:0.7;color:white' data-style='stick' data-ui='false' data-select1='chain:A;resi:11' data-select2='chain:B;resi:7' data-zoomto='chain:A;resi:11' data-labelres1 = '' data-labelres2 = '' data-surface1='opacity:.9;color:red' data-surface2 = 'opacity:.7;color:red'></div></div><div class = 'item' style='background:rgba(255,25.84337584346511,100,0.4);'>A redox-regulated disulphide may form between two units of <b>Insulin</b> at these cysteines.</div><div class = 'item infotitle' style='background:;'>Redox score</div><div class = 'item info' style='background:;'>0.2018306475688695</div><div class = 'item infotitle' style='background:;'>PDB code</div><a class = 'link' href = 'https://www.rcsb.org/structure/1b2d'><div class = 'item info' style='background:;'>1b2d</div></a><div class = 'item infotitle' style='background:;'>Structure name</div><div class = 'item info' style='background:;'>ph affects glu b13 switching and sulfate binding in cubic insulin crystals (ph 6.35 coordinates)</div><div class = 'item infotitle' style='background:;'>Structure deposition date </div><div class = 'item info' style='background:;'>1998-11-26</div><div class = 'item infotitle' style='background:;'>Protein A structure residue number</div><div class = 'item info' style='background:;'>11</div><div class = 'item infotitle' style='background:;'>Protein B structure residue number</div><div class = 'item info' style='background:;'>7</div><div class = 'item infotitle' style='background:;'>Thiol separation</div><div class = 'item info' style='background:;'>9.528171</div><div class = 'item infotitle' style='background:;'>Half-sphere exposure sum</div><div class = 'item info' style='background:;'>52.0</div><div class = 'item infotitle' style='background:;'>Protein A name</div><div class = 'item info' style='background:;'>Insulin</div><div class = 'item infotitle' style='background:;'>Protein A accession</div><a class = 'link' href = 'https://www.uniprot.org/uniprotkb/P01315/entry'><div class = 'item info' style='background:;'>P01315</div></a><div class = 'item infotitle' style='background:;'>Protein A residue number</div><div class = 'item info' style='background:;'>98</div><div class = 'item infotitle' style='background:;'>Protein B name</div><div class = 'item info' style='background:;'>Insulin</div><div class = 'item infotitle' style='background:;'>Protein B accession</div><a class = 'link' href = 'https://www.uniprot.org/uniprotkb/P01315/entry'><div class = 'item info' style='background:;'>P01315</div></a><div class = 'item infotitle' style='background:;'>Protein B residue number</div><div class = 'item info' style='background:;'>31.0</div><div class = 'citation'>If you found this tool useful for finding a disulphide, please cite:<p></div></div><script src='./search.js'></script></body>