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2a9j

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<StructureSection load='2a9j' size='340' side='right'caption='[[2a9j]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2a9j' size='340' side='right'caption='[[2a9j]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2a9j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A9J OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2A9J FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2a9j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A9J FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zst|1zst]], [[1zto|1zto]], [[1zsu|1zsu]], [[2a17|2a17]], [[2a1p|2a1p]], [[2a1q|2a1q]], [[1t8p|1t8p]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1zst|1zst]], [[1zto|1zto]], [[1zsu|1zsu]], [[2a17|2a17]], [[2a1p|2a1p]], [[2a1q|2a1q]], [[1t8p|1t8p]]</div></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/Bisphosphoglycerate_mutase Bisphosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.4 5.4.2.4] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Bisphosphoglycerate_mutase Bisphosphoglycerate mutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.4 5.4.2.4] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2a9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a9j OCA], [http://pdbe.org/2a9j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a9j RCSB], [http://www.ebi.ac.uk/pdbsum/2a9j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2a9j 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=2a9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a9j OCA], [https://pdbe.org/2a9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a9j RCSB], [https://www.ebi.ac.uk/pdbsum/2a9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a9j ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/PMGE_HUMAN PMGE_HUMAN]] Defects in BPGM are the cause of bisphosphoglycerate mutase deficiency (BPGMD) [MIM:[http://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>
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[[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 ==
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[[http://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.
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[[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]]

Revision as of 11:27, 16 February 2022

Human bisphosphoglycerate mutase complexed with 3-phosphoglycerate (17 days)

PDB ID 2a9j

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