This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1vcg
From Proteopedia
(Difference between revisions)
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
==Crystal Structure of IPP isomerase at P43212== | ==Crystal Structure of IPP isomerase at P43212== | ||
| - | <StructureSection load='1vcg' size='340' side='right' caption='[[1vcg]], [[Resolution|resolution]] 3.02Å' scene=''> | + | <StructureSection load='1vcg' size='340' side='right'caption='[[1vcg]], [[Resolution|resolution]] 3.02Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1vcg]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1vcg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VCG FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.02Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |
| - | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vcg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vcg OCA], [https://pdbe.org/1vcg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vcg RCSB], [https://www.ebi.ac.uk/pdbsum/1vcg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vcg ProSAT], [https://www.topsan.org/Proteins/RSGI/1vcg TOPSAN]</span></td></tr> |
| - | + | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/IDI2_THET2 IDI2_THET2] Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).[HAMAP-Rule:MF_00354]<ref>PMID:17428035</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 25: | Line 23: | ||
==See Also== | ==See Also== | ||
*[[Isopentenyl-diphosphate delta-isomerase|Isopentenyl-diphosphate delta-isomerase]] | *[[Isopentenyl-diphosphate delta-isomerase|Isopentenyl-diphosphate delta-isomerase]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Thermus thermophilus]] |
| - | [[Category: Kuramitsu | + | [[Category: Kuramitsu S]] |
| - | [[Category: Park | + | [[Category: Park S-Y]] |
| - | + | [[Category: Tame RH]] | |
| - | [[Category: Tame | + | [[Category: Wada T]] |
| - | [[Category: Wada | + | [[Category: Yokoyama S]] |
| - | [[Category: Yokoyama | + | |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Crystal Structure of IPP isomerase at P43212
| |||||||||||

