2isk
From Proteopedia
(Difference between revisions)
| (6 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:2isk.png|left|200px]] | ||
| - | + | ==BluB bound to flavin anion (charge transfer complex)== | |
| - | + | <StructureSection load='2isk' size='340' side='right'caption='[[2isk]], [[Resolution|resolution]] 2.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2isk]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Sinorhizobium_meliloti Sinorhizobium meliloti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ISK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ISK 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]] 2.1Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FNR:1-DEOXY-1-(7,8-DIMETHYL-2,4-DIOXO-3,4-DIHYDRO-2H-BENZO[G]PTERIDIN-1-ID-10(5H)-YL)-5-O-PHOSPHONATO-D-RIBITOL'>FNR</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=2isk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2isk OCA], [https://pdbe.org/2isk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2isk RCSB], [https://www.ebi.ac.uk/pdbsum/2isk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2isk ProSAT]</span></td></tr> |
| - | [[2isk]] is a 8 chain structure with sequence from [ | + | </table> |
| - | + | == Function == | |
| - | == | + | [https://www.uniprot.org/uniprot/BLUB_RHIME BLUB_RHIME] Involved in the biosynthesis of cobalamin (vitamin B12). Catalyzes the oxidative fragmentation and contraction of the isoalloxazine heterocycle and the cleavage of the ribityl tail of FMN(2) to form 5,6-dimethylbenzimidazole (DMB) and D-erythrose 4-phosphate (E4P). NAD(P)H is only required initially to reduce FMN and oxygen drives the oxidative fragmentation.<ref>PMID:16537439</ref> <ref>PMID:17377583</ref> |
| - | < | + | == Evolutionary Conservation == |
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/is/2isk_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2isk ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Sinorhizobium meliloti]] | [[Category: Sinorhizobium meliloti]] | ||
| - | [[Category: Howard-Jones | + | [[Category: Howard-Jones AR]] |
| - | [[Category: Larsen | + | [[Category: Larsen NA]] |
| - | [[Category: Taga | + | [[Category: Taga ME]] |
| - | [[Category: Walker | + | [[Category: Walker GC]] |
| - | [[Category: Walsh | + | [[Category: Walsh CT]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
BluB bound to flavin anion (charge transfer complex)
| |||||||||||
