5m6z: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

The ~~entry~~ 5m6z is ~~ON HOLD~~

==The X-ray structure of human M189I PGK-1 mutant in partially closed conformation==

~~Authors~~: ~~Ilari~~, A., ~~Fiorillo~~, A., ~~Petrosino~~, M., ~~Cipollone~~, A.

== Structural highlights ==

<table><tr><td colspan='2'>[[5m6z]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M6Z OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M6Z FirstGlance].

~~Description~~: ~~The X-ray structure of human M189I~~ PGK-1 ~~mutant in partially closed conformation~~

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat"><scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>

[[Category: ~~Unreleased Structures~~]]

<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[http://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3] </td></tr>

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5m6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m6z OCA], [http://pdbe.org/5m6z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m6z RCSB], [http://www.ebi.ac.uk/pdbsum/5m6z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m6z ProSAT]</td></tr>

</table>

== Disease ==

[[http://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN]] Defects in PGK1 are the cause of phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:[http://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>

== Function ==

[[http://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 ==

__TOC__

</StructureSection>

[[Category: Phosphoglycerate kinase]]

[[Category: Cipollone, A]]

[[Category: Fiorillo, A]]

[[Category: Ilari, A]]

[[Category: Petrosino, M]]

[[Category: ~~Ilari, A~~]]

[[Category: Human phosphoglycerate kinase 1]]

[[Category: M189i snp -derived mutant]]

[[Category: Transferase]]

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-'''Unreleased structure'''
-The entry 5m6z is ON HOLD
+==The X-ray structure of human M189I PGK-1 mutant in partially closed conformation==
+<StructureSection load='5m6z' size='340' side='right' caption='[[5m6z]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
-Authors: Ilari, A., Fiorillo, A., Petrosino, M., Cipollone, A.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5m6z]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M6Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M6Z FirstGlance]. <br>
-Description: The X-ray structure of human M189I PGK-1 mutant in partially closed conformation
+</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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3] </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=5m6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m6z OCA], [http://pdbe.org/5m6z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m6z RCSB], [http://www.ebi.ac.uk/pdbsum/5m6z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m6z ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[[http://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN]] Defects in PGK1 are the cause of phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:[http://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>
+== Function ==
+[[http://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: Phosphoglycerate kinase]]
 [[Category: Cipollone, A]]
 [[Category: Fiorillo, A]]
+[[Category: Ilari, A]]
 [[Category: Petrosino, M]]
-[[Category: Ilari, A]]
+[[Category: Human phosphoglycerate kinase 1]]
+[[Category: M189i snp -derived mutant]]
+[[Category: Transferase]]