Sandbox Reserved 1132 - Revision history

http://52.214.119.220/wiki/index.php?action=history&feed=atom&title=Sandbox_Reserved_1132 Sandbox Reserved 1132 - Revision history 2026-04-11T11:56:21Z Revision history for this page on the wiki MediaWiki 1.11.2 http://52.214.119.220/wiki/index.php?title=Sandbox_Reserved_1132&diff=2525557&oldid=prev Héloïse Wary at 15:13, 28 January 2016 2016-01-28T15:13:45Z

<p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 15:13, 28 January 2016</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 19:</td> <td colspan="2" class="diff-lineno">Line 19:</td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Structure ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Structure ==</div></td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>FPPS is a dimer made of two identical subunits, which each contain 13 α-helices and connecting loops. The regions which connect the helices α4-α5 and α8-α9 are extended. Within the handle of helices FPPS has a large central cavity, which acts as a hydrophobic ligand-binding site. The site-chain of <scene name='71/719873/Phe_113/1'>Phe-113</scene> limits the cavity on one site. The helices α4 and α8 contain highly conserved and <scene name='71/719873/Aspartate-rich_motives/1'>aspartate-rich motives</scene> (<sup>103</sup>DDIUD<sup>107</sup> and <sup>243</sup>DDYLD<sup>247</sup>). A distinctive kink in helix α7 turns carbonyl of Lys-200 in the direction of the cavity.<ref name = "paper1"> PMID: 16684881 </ref></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>FPPS is a dimer made of two identical subunits, which each contain 13 α-helices and connecting loops. The regions which connect the helices α4-α5 and α8-α9 are extended. Within the handle of helices FPPS has a large central cavity, which acts as a hydrophobic ligand-binding site. The site-chain of <scene name='71/719873/Phe_113/1'>Phe-113</scene> limits the cavity on one site. The helices α4 and α8 contain highly conserved and <scene name='71/719873/Aspartate-rich_motives/1'>aspartate-rich motives</scene> (<sup>103</sup>DDIUD<sup>107</sup> and <sup>243</sup>DDYLD<sup>247</sup>). A distinctive kink in helix α7 turns carbonyl of <ins style="color: red; font-weight: bold; text-decoration: none;"><scene name='71/719873/</ins>Lys-200<ins style="color: red; font-weight: bold; text-decoration: none;">/1'>Lys-200</scene> </ins>in the direction of the cavity.<ref name = "paper1"> PMID: 16684881 </ref></div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> </table>

Héloïse Wary http://52.214.119.220/wiki/index.php?title=Sandbox_Reserved_1132&diff=2525555&oldid=prev Héloïse Wary at 15:09, 28 January 2016 2016-01-28T15:09:20Z

<p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 15:09, 28 January 2016</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 28:</td> <td colspan="2" class="diff-lineno">Line 28:</td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>====Interactions with nitrogen-containing bisphosphonates (N-BP) ====</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>====Interactions with nitrogen-containing bisphosphonates (N-BP) ====</div></td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>The side chain is located in the hydrophobic cleft that normally accomodates an isoprenoid lipid, and the phosphonate groups are bound to a cluster of three Mg<sup>2+</sup> ions, which were chelated by two <del style="color: red; font-weight: bold; text-decoration: none;">asparate</del>-rich <del style="color: red; font-weight: bold; text-decoration: none;">motifs</del>.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>The side chain is located in the hydrophobic cleft that normally accomodates an isoprenoid lipid, and the phosphonate groups are bound to a cluster of three Mg<sup>2+</sup> ions, which were chelated by two <ins style="color: red; font-weight: bold; text-decoration: none;"><scene name='71/719873/Aspartate-rich_motives/1'>aspartate</ins>-rich <ins style="color: red; font-weight: bold; text-decoration: none;">motives</scene></ins>.</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>There is a large cavity in the helical bundle that forms a partly hydrophobic ligand-binding site. This cavity is delimited by <scene name='71/719873/Phe_113/1'>Phe-113</scene> .<ref name = "paper1" > </ref></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>There is a large cavity in the helical bundle that forms a partly hydrophobic ligand-binding site. This cavity is delimited by <scene name='71/719873/Phe_113/1'>Phe-113</scene> .<ref name = "paper1" > </ref></div></td></tr> </table>

Héloïse Wary http://52.214.119.220/wiki/index.php?title=Sandbox_Reserved_1132&diff=2525554&oldid=prev Héloïse Wary at 15:08, 28 January 2016 2016-01-28T15:08:31Z

<p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 15:08, 28 January 2016</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 19:</td> <td colspan="2" class="diff-lineno">Line 19:</td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Structure ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Structure ==</div></td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>FPPS is a dimer made of two identical subunits, which each contain 13 α-helices and connecting loops. The regions which connect the helices α4-α5 and α8-α9 are extended. Within the handle of helices FPPS has a large central cavity, which acts as a hydrophobic ligand-binding site. The site-chain of Phe-113 limits the cavity on one site. The helices α4 and α8 contain highly conserved and <scene name='71/719873/Aspartate-rich_motives/1'>aspartate-rich motives</scene> (<sup>103</sup>DDIUD<sup>107</sup> and <sup>243</sup>DDYLD<sup>247</sup>). A distinctive kink in helix α7 turns carbonyl of Lys-200 in the direction of the cavity.<ref name = "paper1"> PMID: 16684881 </ref></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>FPPS is a dimer made of two identical subunits, which each contain 13 α-helices and connecting loops. The regions which connect the helices α4-α5 and α8-α9 are extended. Within the handle of helices FPPS has a large central cavity, which acts as a hydrophobic ligand-binding site. The site-chain of <ins style="color: red; font-weight: bold; text-decoration: none;"><scene name='71/719873/Phe_113/1'></ins>Phe-113<ins style="color: red; font-weight: bold; text-decoration: none;"></scene> </ins>limits the cavity on one site. The helices α4 and α8 contain highly conserved and <scene name='71/719873/Aspartate-rich_motives/1'>aspartate-rich motives</scene> (<sup>103</sup>DDIUD<sup>107</sup> and <sup>243</sup>DDYLD<sup>247</sup>). A distinctive kink in helix α7 turns carbonyl of Lys-200 in the direction of the cavity.<ref name = "paper1"> PMID: 16684881 </ref></div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> </table>

Héloïse Wary http://52.214.119.220/wiki/index.php?title=Sandbox_Reserved_1132&diff=2525552&oldid=prev Héloïse Wary at 15:07, 28 January 2016 2016-01-28T15:07:13Z

<p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 15:07, 28 January 2016</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 19:</td> <td colspan="2" class="diff-lineno">Line 19:</td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Structure ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Structure ==</div></td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>FPPS is a dimer made of two identical subunits, which each contain 13 α-helices and connecting loops. The regions which connect the helices α4-α5 and α8-α9 are extended. Within the handle of helices FPPS has a large central cavity, which acts as a hydrophobic ligand-binding site. The site-chain of Phe-113 limits the cavity on one site. The helices α4 and α8 contain highly conserved and <del style="color: red; font-weight: bold; text-decoration: none;">aspartate-rich motives (<sup>103</sup></del><scene name='71/719873/<del style="color: red; font-weight: bold; text-decoration: none;">103</del>-<del style="color: red; font-weight: bold; text-decoration: none;">107</del>/1'><del style="color: red; font-weight: bold; text-decoration: none;">DDIUD</del></scene><sup>107</sup> and <sup>243</sup>DDYLD<sup>247</sup>). A distinctive kink in helix α7 turns carbonyl of Lys-200 in the direction of the cavity.<ref name = "paper1"> PMID: 16684881 </ref></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>FPPS is a dimer made of two identical subunits, which each contain 13 α-helices and connecting loops. The regions which connect the helices α4-α5 and α8-α9 are extended. Within the handle of helices FPPS has a large central cavity, which acts as a hydrophobic ligand-binding site. The site-chain of Phe-113 limits the cavity on one site. The helices α4 and α8 contain highly conserved and <scene name='71/719873/<ins style="color: red; font-weight: bold; text-decoration: none;">Aspartate</ins>-<ins style="color: red; font-weight: bold; text-decoration: none;">rich_motives</ins>/1'><ins style="color: red; font-weight: bold; text-decoration: none;">aspartate-rich motives</ins></scene> <ins style="color: red; font-weight: bold; text-decoration: none;">(<sup>103</sup>DDIUD</ins><sup>107</sup> and <sup>243</sup>DDYLD<sup>247</sup>). A distinctive kink in helix α7 turns carbonyl of Lys-200 in the direction of the cavity.<ref name = "paper1"> PMID: 16684881 </ref></div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> </table>

Héloïse Wary http://52.214.119.220/wiki/index.php?title=Sandbox_Reserved_1132&diff=2525551&oldid=prev Héloïse Wary at 15:02, 28 January 2016 2016-01-28T15:02:32Z

<p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 15:02, 28 January 2016</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 19:</td> <td colspan="2" class="diff-lineno">Line 19:</td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Structure ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Structure ==</div></td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>FPPS is a dimer made of two identical subunits, which each contain 13 α-helices and connecting loops. The regions which connect the helices α4-α5 and α8-α9 are extended. Within the handle of helices FPPS has a large central cavity, which acts as a hydrophobic ligand-binding site. The site-chain of Phe-113 limits the cavity on one site. The helices α4 and α8 contain highly conserved and aspartate-rich motives (<sup>103</sup>DDIUD<sup>107</sup> and <sup>243</sup>DDYLD<sup>247</sup>). A distinctive kink in helix α7 turns carbonyl of Lys-200 in the direction of the cavity.<ref name = "paper1"> PMID: 16684881 </ref></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>FPPS is a dimer made of two identical subunits, which each contain 13 α-helices and connecting loops. The regions which connect the helices α4-α5 and α8-α9 are extended. Within the handle of helices FPPS has a large central cavity, which acts as a hydrophobic ligand-binding site. The site-chain of Phe-113 limits the cavity on one site. The helices α4 and α8 contain highly conserved and aspartate-rich motives (<sup>103</sup<ins style="color: red; font-weight: bold; text-decoration: none;">><scene name='71/719873/103-107/1'</ins>>DDIUD<ins style="color: red; font-weight: bold; text-decoration: none;"></scene></ins><sup>107</sup> and <sup>243</sup>DDYLD<sup>247</sup>). A distinctive kink in helix α7 turns carbonyl of Lys-200 in the direction of the cavity.<ref name = "paper1"> PMID: 16684881 </ref></div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> </table>

Héloïse Wary http://52.214.119.220/wiki/index.php?title=Sandbox_Reserved_1132&diff=2525541&oldid=prev Héloïse Wary at 14:52, 28 January 2016 2016-01-28T14:52:19Z

<p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 14:52, 28 January 2016</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 1:</td> <td colspan="2" class="diff-lineno">Line 1:</td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''Bold text'''<Structure load='3N5J' size='350' frame='true' align='right' caption='Human Farnesyl pyrophosphate synthase, resolution 1.60Å' scene='Insert optional scene name here' />{{Sandbox_Reserved_ESBS_2015}}</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>'''Bold text'''<Structure load='3N5J' size='350' frame='true' align='right' caption='Human Farnesyl pyrophosphate synthase, resolution 1.60Å' scene='Insert optional scene name here' />{{Sandbox_Reserved_ESBS_2015}}</div></td></tr> <tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"></td></tr> <tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td colspan="2" class="diff-lineno">Line 28:</td> <td colspan="2" class="diff-lineno">Line 30:</td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The side chain is located in the hydrophobic cleft that normally accomodates an isoprenoid lipid, and the phosphonate groups are bound to a cluster of three Mg<sup>2+</sup> ions, which were chelated by two asparate-rich motifs.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The side chain is located in the hydrophobic cleft that normally accomodates an isoprenoid lipid, and the phosphonate groups are bound to a cluster of three Mg<sup>2+</sup> ions, which were chelated by two asparate-rich motifs.</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>There is a large cavity in the helical bundle that forms a partly hydrophobic ligand-binding site. This cavity is delimited by Phe-113.<ref name = "paper1" > </ref></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>There is a large cavity in the helical bundle that forms a partly hydrophobic ligand-binding site. This cavity is delimited by <ins style="color: red; font-weight: bold; text-decoration: none;"><scene name='71/719873/Phe_113/1'></ins>Phe-113<ins style="color: red; font-weight: bold; text-decoration: none;"></scene> </ins>.<ref name = "paper1" > </ref></div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>N-BP binding causes a structural rearrangement and a decrease of size in the internal cavity. The movement is mediated by α4 and α8 which participate in the ligand binding. Many connections occur in this movement : residues 249-268 bind over the N-BP and stay in place because of polar interactions : loop residue Lys-257 contacts Asp-243 and a phosphonate oxygen. Asp-247 at the end of α8 forms bidentate hydrogen bonds with main-chain amides of Thr-260 and Asp-261. The main chain from Ile-258 to Thr-260 is separated. The heterocyclic ring structures of RIS and ZOL are surrounded mainly by hydrophobic side chains of residues Phe-99, Leu-100, Thr-167, Lys-200, and Tyr-204, and the nitrogen atom of the ring system is found within hydrogen-bonding. There is a network of salt links involving Lys-57, the terminal carboxylate of Lys-353, and Arg-351.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>N-BP binding causes a structural rearrangement and a decrease of size in the internal cavity. The movement is mediated by α4 and α8 which participate in the ligand binding. Many connections occur in this movement : residues 249-268 bind over the N-BP and stay in place because of polar interactions : loop residue Lys-257 contacts Asp-243 and a phosphonate oxygen. Asp-247 at the end of α8 forms bidentate hydrogen bonds with main-chain amides of Thr-260 and Asp-261. The main chain from Ile-258 to Thr-260 is separated. The heterocyclic ring structures of RIS and ZOL are surrounded mainly by hydrophobic side chains of residues Phe-99, Leu-100, Thr-167, Lys-200, and Tyr-204, and the nitrogen atom of the ring system is found within hydrogen-bonding. There is a network of salt links involving Lys-57, the terminal carboxylate of Lys-353, and Arg-351.</div></td></tr> </table>

Héloïse Wary http://52.214.119.220/wiki/index.php?title=Sandbox_Reserved_1132&diff=2525530&oldid=prev Héloïse Wary at 14:42, 28 January 2016 2016-01-28T14:42:10Z

<p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 14:42, 28 January 2016</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 2:</td> <td colspan="2" class="diff-lineno">Line 2:</td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>Human Farnesyl pyrophoasphate synthase (FPPS) is a transferase, which belongs to the Trans-Isoprenyl Diphosphate Synthases family. It is an important enzyme in isoprenoid synthesis, which catalyses the formation of farmesyl diphosphate (FPP). FPP is a precursor for important metabolizes like sterols, dolichols and ubiquinones.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><ins style="color: red; font-weight: bold; text-decoration: none;">'''</ins>Human Farnesyl pyrophoasphate synthase (FPPS)<ins style="color: red; font-weight: bold; text-decoration: none;">''' </ins>is a transferase, which belongs to the Trans-Isoprenyl Diphosphate Synthases family. It is an important enzyme in isoprenoid synthesis, which catalyses the formation of farmesyl diphosphate (FPP). FPP is a precursor for important metabolizes like sterols, dolichols and ubiquinones.</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><table><tr><td colspan='2'></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><table><tr><td colspan='2'></div></td></tr> </table>

Héloïse Wary http://52.214.119.220/wiki/index.php?title=Sandbox_Reserved_1132&diff=2525528&oldid=prev Héloïse Wary at 14:41, 28 January 2016 2016-01-28T14:41:29Z

<p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 14:41, 28 January 2016</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 4:</td> <td colspan="2" class="diff-lineno">Line 4:</td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Human Farnesyl pyrophoasphate synthase (FPPS) is a transferase, which belongs to the Trans-Isoprenyl Diphosphate Synthases family. It is an important enzyme in isoprenoid synthesis, which catalyses the formation of farmesyl diphosphate (FPP). FPP is a precursor for important metabolizes like sterols, dolichols and ubiquinones.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Human Farnesyl pyrophoasphate synthase (FPPS) is a transferase, which belongs to the Trans-Isoprenyl Diphosphate Synthases family. It is an important enzyme in isoprenoid synthesis, which catalyses the formation of farmesyl diphosphate (FPP). FPP is a precursor for important metabolizes like sterols, dolichols and ubiquinones.</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><table><tr><td colspan='2'<del style="color: red; font-weight: bold; text-decoration: none;">>[[3n5j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N5J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3N5J FirstGlance]. <br</del>></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><table><tr><td colspan='2'></div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div></td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GO1:3-(CARBOXYMETHYL)-5,7-DICHLORO-1H-INDOLE-2-CARBOXYLIC+ACID'>GO1</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div></td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GO1:3-(CARBOXYMETHYL)-5,7-DICHLORO-1H-INDOLE-2-CARBOXYLIC+ACID'>GO1</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr></div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3n1v|3n1v]], [[3n1w|3n1w]], [[3n3l|3n3l]], [[3n45|3n45]], [[3n46|3n46]], [[3n49|3n49]], [[3n5h|3n5h]], [[3n6k|3n6k]]</td></tr></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3n1v|3n1v]], [[3n1w|3n1w]], [[3n3l|3n3l]], [[3n45|3n45]], [[3n46|3n46]], [[3n49|3n49]], [[3n5h|3n5h]], [[3n6k|3n6k]]</td></tr></div></td></tr> <tr><td colspan="2" class="diff-lineno">Line 10:</td> <td colspan="2" class="diff-lineno">Line 10:</td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><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=3n5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n5j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3n5j RCSB], [http://www.ebi.ac.uk/pdbsum/3n5j PDBsum]</span></td></tr></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><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=3n5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n5j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3n5j RCSB], [http://www.ebi.ac.uk/pdbsum/3n5j PDBsum]</span></td></tr></div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div></table></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div></table></div></td></tr> <tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Family ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Family ==</div></td></tr> </table>

Héloïse Wary http://52.214.119.220/wiki/index.php?title=Sandbox_Reserved_1132&diff=2525526&oldid=prev Héloïse Wary at 14:39, 28 January 2016 2016-01-28T14:39:41Z

<p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 14:39, 28 January 2016</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 4:</td> <td colspan="2" class="diff-lineno">Line 4:</td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Human Farnesyl pyrophoasphate synthase (FPPS) is a transferase, which belongs to the Trans-Isoprenyl Diphosphate Synthases family. It is an important enzyme in isoprenoid synthesis, which catalyses the formation of farmesyl diphosphate (FPP). FPP is a precursor for important metabolizes like sterols, dolichols and ubiquinones.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>Human Farnesyl pyrophoasphate synthase (FPPS) is a transferase, which belongs to the Trans-Isoprenyl Diphosphate Synthases family. It is an important enzyme in isoprenoid synthesis, which catalyses the formation of farmesyl diphosphate (FPP). FPP is a precursor for important metabolizes like sterols, dolichols and ubiquinones.</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><table><tr><td colspan='2'>[[3n5j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N5J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3N5J FirstGlance]. <br></div></td></tr> <tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div></td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GO1:3-(CARBOXYMETHYL)-5,7-DICHLORO-1H-INDOLE-2-CARBOXYLIC+ACID'>GO1</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr></div></td></tr> <tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3n1v|3n1v]], [[3n1w|3n1w]], [[3n3l|3n3l]], [[3n45|3n45]], [[3n46|3n46]], [[3n49|3n49]], [[3n5h|3n5h]], [[3n6k|3n6k]]</td></tr></div></td></tr> <tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FDPS, FPS, KIAA1293 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr></div></td></tr> <tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><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=3n5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n5j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3n5j RCSB], [http://www.ebi.ac.uk/pdbsum/3n5j PDBsum]</span></td></tr></div></td></tr> <tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div></table></div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Family ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Family ==</div></td></tr> </table>

Héloïse Wary http://52.214.119.220/wiki/index.php?title=Sandbox_Reserved_1132&diff=2525517&oldid=prev Héloïse Wary at 14:33, 28 January 2016 2016-01-28T14:33:12Z

<p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 14:33, 28 January 2016</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 1:</td> <td colspan="2" class="diff-lineno">Line 1:</td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>'''Bold text'''<Structure load='3N5J' size='350' frame='true' align='right' caption='<del style="color: red; font-weight: bold; text-decoration: none;">Insert caption here</del>' scene='Insert optional scene name here' />{{Sandbox_Reserved_ESBS_2015}}</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>'''Bold text'''<Structure load='3N5J' size='350' frame='true' align='right' caption='<ins style="color: red; font-weight: bold; text-decoration: none;">Human Farnesyl pyrophosphate synthase, resolution 1.60Å</ins>' scene='Insert optional scene name here' />{{Sandbox_Reserved_ESBS_2015}}</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> </table>

Héloïse Wary