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5yft

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==Crystal structure of ribose-1,5-bisphosphate isomerase mutant D204N from Pyrococcus horikoshii OT3 in complex with ribose-1,5-bisphosphate==
==Crystal structure of ribose-1,5-bisphosphate isomerase mutant D204N from Pyrococcus horikoshii OT3 in complex with ribose-1,5-bisphosphate==
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<StructureSection load='5yft' size='340' side='right' caption='[[5yft]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
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<StructureSection load='5yft' size='340' side='right'caption='[[5yft]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5yft]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YFT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YFT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5yft]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YFT FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=RI2:1,5-DI-O-PHOSPHONO-ALPHA-D-RIBOFURANOSE'>RI2</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribose_1,5-bisphosphate_isomerase Ribose 1,5-bisphosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.29 5.3.1.29] </span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=RI2:1,5-DI-O-PHOSPHONO-ALPHA-D-RIBOFURANOSE'>RI2</scene></td></tr>
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<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=5yft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yft OCA], [http://pdbe.org/5yft PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yft RCSB], [http://www.ebi.ac.uk/pdbsum/5yft PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yft ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5yft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yft OCA], [https://pdbe.org/5yft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yft RCSB], [https://www.ebi.ac.uk/pdbsum/5yft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yft ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/R15PI_PYRHO R15PI_PYRHO]] Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P) to ribulose 1,5-bisphosphate (RuBP), the CO(2) acceptor and substrate for RubisCO. Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and RubisCO (By similarity).
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[https://www.uniprot.org/uniprot/R15PI_PYRHO R15PI_PYRHO] Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P) to ribulose 1,5-bisphosphate (RuBP), the CO(2) acceptor and substrate for RubisCO. Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and RubisCO (By similarity).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ribose 1,5-bisphosphate isomerase]]
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[[Category: Large Structures]]
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[[Category: Gogoi, P]]
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[[Category: Pyrococcus horikoshii OT3]]
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[[Category: Kanaujia, S P]]
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[[Category: Gogoi P]]
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[[Category: 5-bisphosphate]]
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[[Category: Kanaujia SP]]
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[[Category: Isomerase]]
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[[Category: Nmp degradation pathway]]
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[[Category: Ribose-1]]
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[[Category: Rossmann-like fold]]
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Current revision

Crystal structure of ribose-1,5-bisphosphate isomerase mutant D204N from Pyrococcus horikoshii OT3 in complex with ribose-1,5-bisphosphate

PDB ID 5yft

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