9fdh: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
Line 1: Line 1:
'''Unreleased structure'''


The entry 9fdh is ON HOLD  until Paper Publication
==Closed Human phosphoglycerate kinase complex with BPG and ADP produced by cross-soaking a TSA crystal==
 
<StructureSection load='9fdh' size='340' side='right'caption='[[9fdh]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
Authors: Cliff, M.J., Waltho, J.P., Bowler, M.W., Baxter, N.J., Bisson, C., Blackburn, G.M.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[9fdh]] is a 1 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=9FDH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FDH FirstGlance]. <br>
Description: Closed Human phosphoglycerate kinase complex with BPG and ADP produced by cross-soaking a TSA crystal
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.756&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=X15:1,3-BISPHOSPHOGLYCERIC+ACID'>X15</scene></td></tr>
[[Category: Cliff, M.J]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9fdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9fdh OCA], [https://pdbe.org/9fdh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9fdh RCSB], [https://www.ebi.ac.uk/pdbsum/9fdh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9fdh ProSAT]</span></td></tr>
[[Category: Baxter, N.J]]
</table>
[[Category: Bisson, C]]
== Disease ==
[[Category: Waltho, J.P]]
[https://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN] Defects in PGK1 are the cause of phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:[https://omim.org/entry/300653 300653]. It is a condition with a highly variable clinical phenotype that includes hemolytic anemia, rhabdomyolysis, myopathy and neurologic involvement. Patients can express one or more of these manifestations.<ref>PMID:8673469</ref> <ref>PMID:8043870</ref> <ref>PMID:8615693</ref> <ref>PMID:9744480</ref> <ref>PMID:2001457</ref> <ref>PMID:1586722</ref> <ref>PMID:1547346</ref> <ref>PMID:6941312</ref> <ref>PMID:6933565</ref>
[[Category: Bowler, M.W]]
== Function ==
[[Category: Blackburn, G.M]]
[https://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN] In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein).
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Baxter NJ]]
[[Category: Bisson C]]
[[Category: Blackburn GM]]
[[Category: Bowler MW]]
[[Category: Cliff MJ]]
[[Category: Waltho JP]]