7thi
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Human Bisphosphoglycerate Mutase complexed with 2-phosphoglycolate== | |
| - | + | <StructureSection load='7thi' size='340' side='right'caption='[[7thi]], [[Resolution|resolution]] 1.33Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[7thi]] 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=7THI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7THI 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]] 1.33Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr> |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7thi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7thi OCA], [https://pdbe.org/7thi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7thi RCSB], [https://www.ebi.ac.uk/pdbsum/7thi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7thi ProSAT]</span></td></tr> |
| - | [[Category: | + | </table> |
| - | [[Category: | + | == Disease == |
| - | [[Category: | + | [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> |
| - | [[Category: | + | == Function == |
| - | [[Category: | + | [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. |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Christodoulou C]] | ||
| + | [[Category: Clark KL]] | ||
| + | [[Category: Isome Y]] | ||
| + | [[Category: Kulathila R]] | ||
| + | [[Category: Sage D]] | ||
| + | [[Category: Wright K]] | ||
| + | [[Category: Yang Y]] | ||
Current revision
Human Bisphosphoglycerate Mutase complexed with 2-phosphoglycolate
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Categories: Homo sapiens | Large Structures | Christodoulou C | Clark KL | Isome Y | Kulathila R | Sage D | Wright K | Yang Y
