3a11
From Proteopedia
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| - | {{STRUCTURE_3a11| PDB=3a11 | SCENE= }} | ||
| - | ===Crystal structure of ribose-1,5-bisphosphate isomerase from Thermococcus kodakaraensis KOD1=== | ||
| - | {{ABSTRACT_PUBMED_22511789}} | ||
| - | == | + | ==Crystal structure of ribose-1,5-bisphosphate isomerase from Thermococcus kodakaraensis KOD1== |
| - | [[3a11]] is a 6 chain structure with sequence from [ | + | <StructureSection load='3a11' size='340' side='right'caption='[[3a11]], [[Resolution|resolution]] 2.50Å' scene=''> |
| - | + | == Structural highlights == | |
| - | == | + | <table><tr><td colspan='2'>[[3a11]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis_KOD1 Thermococcus kodakarensis KOD1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A11 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A11 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]] 2.5Å</td></tr> |
| - | [[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=3a11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a11 OCA], [https://pdbe.org/3a11 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a11 RCSB], [https://www.ebi.ac.uk/pdbsum/3a11 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a11 ProSAT]</span></td></tr> |
| - | [[ | + | </table> |
| - | [[Category: | + | == Function == |
| - | [[Category: | + | [https://www.uniprot.org/uniprot/R15PI_THEKO R15PI_THEKO] Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P) to ribulose 1,5-bisphosphate (RuBP), the CO(2) acceptor and substrate for RubisCO. Only accepts the alpha-anomer of D-ribose 1,5-bisphosphate as substrate, being inactive on the beta-anomer. Displays a strict substrate specificity, since other phosphorylated sugars such as R5P, ribose, G16P, G6P, G1P, FBP, F6P, and PRPP, are not substrates. Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and RubisCO.<ref>PMID:17303759</ref> <ref>PMID:22511789</ref> <ref>PMID:23065974</ref> |
| - | [[Category: | + | == Evolutionary Conservation == |
| - | [[Category: | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | [[Category: | + | Check<jmol> |
| - | [[Category: | + | <jmolCheckbox> |
| - | [[Category: | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a1/3a11_consurf.spt"</scriptWhenChecked> |
| - | [[Category: | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | [[Category: | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | [[Category: | + | </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=3a11 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermococcus kodakarensis KOD1]] | ||
| + | [[Category: Atomi H]] | ||
| + | [[Category: Fujihashi M]] | ||
| + | [[Category: Imanaka T]] | ||
| + | [[Category: Miki K]] | ||
| + | [[Category: Nakamura A]] | ||
| + | [[Category: Nishiba Y]] | ||
| + | [[Category: Yano A]] | ||
| + | [[Category: Yoshida S]] | ||
Current revision
Crystal structure of ribose-1,5-bisphosphate isomerase from Thermococcus kodakaraensis KOD1
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