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1t8p
From Proteopedia
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==Crystal structure of Human erythrocyte 2,3-bisphosphoglycerate mutase== | ==Crystal structure of Human erythrocyte 2,3-bisphosphoglycerate mutase== | ||
| - | <StructureSection load='1t8p' size='340' side='right' caption='[[1t8p]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='1t8p' size='340' side='right'caption='[[1t8p]], [[Resolution|resolution]] 2.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1t8p]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1t8p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T8P FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b> | + | </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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t8p OCA], [https://pdbe.org/1t8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t8p RCSB], [https://www.ebi.ac.uk/pdbsum/1t8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t8p ProSAT]</span></td></tr> |
| - | <table> | + | </table> |
== Disease == | == Disease == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/PMGE_HUMAN PMGE_HUMAN] Defects in BPGM are the cause of bisphosphoglycerate mutase deficiency (BPGMD) [MIM:[https://omim.org/entry/222800 222800]. A disease characterized by hemolytic anemia, splenomegaly, cholelithiasis and cholecystitis.<ref>PMID:2542247</ref> <ref>PMID:1421379</ref> <ref>PMID:15054810</ref> |
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/PMGE_HUMAN PMGE_HUMAN] Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.1) and phosphatase (EC 3.1.3.13) activities. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t8/1t8p_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t8/1t8p_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=1t8p ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 1t8p" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Phosphoglycerate | + | *[[Phosphoglycerate mutase 3D structures|Phosphoglycerate mutase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Bisphosphoglycerate mutase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Bian | + | [[Category: Large Structures]] |
| - | [[Category: Cheng | + | [[Category: Bian Q]] |
| - | [[Category: Gong | + | [[Category: Cheng Z]] |
| - | [[Category: Liu | + | [[Category: Gong W]] |
| - | [[Category: Wan | + | [[Category: Liu L]] |
| - | [[Category: Wang | + | [[Category: Wan M]] |
| - | [[Category: Wei | + | [[Category: Wang Y]] |
| - | + | [[Category: Wei Z]] | |
Current revision
Crystal structure of Human erythrocyte 2,3-bisphosphoglycerate mutase
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Categories: Homo sapiens | Large Structures | Bian Q | Cheng Z | Gong W | Liu L | Wan M | Wang Y | Wei Z
