1xdp
From Proteopedia
(Difference between revisions)
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<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=1xdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xdp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xdp RCSB], [http://www.ebi.ac.uk/pdbsum/1xdp 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=1xdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xdp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xdp RCSB], [http://www.ebi.ac.uk/pdbsum/1xdp PDBsum]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/PPK_ECOLI PPK_ECOLI]] Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Can form linear polymers of orthophosphate with chain lengths up to 1000 or more. Can also act in the reverse direction to form ATP in the presence of excess ADP. Can also use GTP instead of ATP; but the efficiency of GTP is 5% that of ATP.<ref>PMID:8962061</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] |
Revision as of 21:30, 25 December 2014
Crystal Structure of the E.coli Polyphosphate Kinase in complex with AMPPNP
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