2hhj

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Current revision (22:23, 26 March 2025) (edit) (undo)
 
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<StructureSection load='2hhj' size='340' side='right'caption='[[2hhj]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='2hhj' size='340' side='right'caption='[[2hhj]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2hhj]] 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=2HHJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HHJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2hhj]] 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=2HHJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HHJ FirstGlance]. <br>
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</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>, <scene name='pdbligand=DG2:(2R)-2,3-DIPHOSPHOGLYCERIC+ACID'>DG2</scene>, <scene name='pdbligand=HAI:CYCLOHEXYLAMMONIUM+ION'>HAI</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]] 1.5&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene></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=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=DG2:(2R)-2,3-DIPHOSPHOGLYCERIC+ACID'>DG2</scene>, <scene name='pdbligand=HAI:CYCLOHEXYLAMMONIUM+ION'>HAI</scene>, <scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene></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;'>[[1t8p|1t8p]], [[2h52|2h52]]</div></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=2hhj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hhj OCA], [https://pdbe.org/2hhj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hhj RCSB], [https://www.ebi.ac.uk/pdbsum/2hhj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hhj ProSAT]</span></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=2hhj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hhj OCA], [https://pdbe.org/2hhj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hhj RCSB], [https://www.ebi.ac.uk/pdbsum/2hhj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hhj ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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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>
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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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[[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.
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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]]
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<jmolCheckbox>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hh/2hhj_consurf.spt"</scriptWhenChecked>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hh/2hhj_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gong, W]]
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[[Category: Gong W]]
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[[Category: Wang, Y]]
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[[Category: Wang Y]]
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[[Category: 3-bisphosphoglycerate]]
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[[Category: Bisphosphoglycerate mutase]]
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[[Category: Isomerase]]
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Current revision

Human bisphosphoglycerate mutase complexed with 2,3-bisphosphoglycerate (15 days)

PDB ID 2hhj

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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