2h52: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2h52]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H52 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2h52]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H52 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=HAI:CYCLOHEXYLAMMONIUM+ION'>HAI</scene><br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=HAI:CYCLOHEXYLAMMONIUM+ION'>HAI</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2h4x|2h4x]], [[2h4z|2h4z]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2h4x|2h4x]], [[2h4z|2h4z]]</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h52 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2h52 RCSB], [http://www.ebi.ac.uk/pdbsum/2h52 PDBsum]</span></td></tr>
<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=2h52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h52 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2h52 RCSB], [http://www.ebi.ac.uk/pdbsum/2h52 PDBsum]</span></td></tr>
<table>
</table>
== Disease ==
== Disease ==
[[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>   
[[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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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Gong, W.]]
[[Category: Gong, W]]
[[Category: Wang, Y.]]
[[Category: Wang, Y]]
[[Category: 3-phosphoglycerate]]
[[Category: 3-phosphoglycerate]]
[[Category: Bisphosphoglycerate mutase]]
[[Category: Bisphosphoglycerate mutase]]
[[Category: Isomerase]]
[[Category: Isomerase]]

Revision as of 12:23, 16 January 2015

Crystal structure of human bisphosphoglycerate mutase complex with 3-phosphoglycerate (18 days)Crystal structure of human bisphosphoglycerate mutase complex with 3-phosphoglycerate (18 days)

Structural highlights

2h52 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, RCSB, PDBsum

Disease

[PMGE_HUMAN] Defects in BPGM are the cause of bisphosphoglycerate mutase deficiency (BPGMD) [MIM:222800]. A disease characterized by hemolytic anemia, splenomegaly, cholelithiasis and cholecystitis.[1] [2] [3]

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Rosa R, Blouquit Y, Calvin MC, Prome D, Prome JC, Rosa J. Isolation, characterization, and structure of a mutant 89 Arg----Cys bisphosphoglycerate mutase. Implication of the active site in the mutation. J Biol Chem. 1989 May 15;264(14):7837-43. PMID:2542247
  2. Lemarchandel V, Joulin V, Valentin C, Rosa R, Galacteros F, Rosa J, Cohen-Solal M. Compound heterozygosity in a complete erythrocyte bisphosphoglycerate mutase deficiency. Blood. 1992 Nov 15;80(10):2643-9. PMID:1421379
  3. Hoyer JD, Allen SL, Beutler E, Kubik K, West C, Fairbanks VF. Erythrocytosis due to bisphosphoglycerate mutase deficiency with concurrent glucose-6-phosphate dehydrogenase (G-6-PD) deficiency. Am J Hematol. 2004 Apr;75(4):205-8. PMID:15054810 doi:10.1002/ajh.20014

2h52, resolution 2.00Å

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