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1yfk
From Proteopedia
(Difference between revisions)
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<StructureSection load='1yfk' size='340' side='right'caption='[[1yfk]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='1yfk' size='340' side='right'caption='[[1yfk]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1yfk]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1yfk]] 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=1YFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YFK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yfk OCA], [https://pdbe.org/1yfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yfk RCSB], [https://www.ebi.ac.uk/pdbsum/1yfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yfk ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/PGAM1_HUMAN PGAM1_HUMAN]] Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 16:27, 3 November 2021
Crystal structure of human B type phosphoglycerate mutase
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Categories: Human | Large Structures | Gong, W | Liu, L | Wang, Y | Wei, Z | Alpha/beta | Hydrolase | Isomerase

