1ndp
From Proteopedia
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<StructureSection load='1ndp' size='340' side='right'caption='[[1ndp]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1ndp' size='340' side='right'caption='[[1ndp]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1ndp]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1ndp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NDP FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
- | <tr id=' | + | <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=MG:MAGNESIUM+ION'>MG</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=1ndp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ndp OCA], [https://pdbe.org/1ndp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ndp RCSB], [https://www.ebi.ac.uk/pdbsum/1ndp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ndp ProSAT]</span></td></tr> |
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/NDKC_DICDI NDKC_DICDI] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ndp ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ndp ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The X-ray structure of nucleoside diphosphate kinase (NDP kinase) from the slime mold Dictyostelium discoideum has been determined to 2.2-A resolution and refined to an R-factor of 0.19 with and without bound ADP-Mg2+. The nucleotide binds near His 122, a residue which becomes phosphorylated during the catalytic cycle. The mode of binding is different from that observed in other phosphokinases, and it involves no glycine-rich sequence. The adenine base makes only nonpolar contacts with the protein. It points outside, explaining the lack of specificity of NDP kinase toward the base. The ribose 2'- and 3'-hydroxyls and the pyrophosphate moiety are H-bonded to polar side chains. A Mg2+ ion bridges the alpha- to the beta-phosphate which approaches the imidazole group of His 122 from the N delta side. The geometry at the active site in the ADP-Mg2+ complex suggests a mechanism for catalysis whereby the gamma-phosphate of a nucleoside triphosphate can be transferred onto His 122 with a minimum of atomic motion. | ||
- | |||
- | Adenosine 5'-diphosphate binding and the active site of nucleoside diphosphate kinase.,Morera S, Lascu I, Dumas C, LeBras G, Briozzo P, Veron M, Janin J Biochemistry. 1994 Jan 18;33(2):459-67. PMID:8286376<ref>PMID:8286376</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1ndp" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Nucleoside diphosphate kinase 3D structures|Nucleoside diphosphate kinase 3D structures]] | *[[Nucleoside diphosphate kinase 3D structures|Nucleoside diphosphate kinase 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Dictyostelium discoideum]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | + | [[Category: Dumas C]] | |
- | [[Category: Dumas | + | [[Category: Janin J]] |
- | [[Category: Janin | + | [[Category: Lascu I]] |
- | [[Category: Lascu | + | [[Category: Lebras G]] |
- | [[Category: Lebras | + | [[Category: Morera S]] |
- | [[Category: Morera | + | [[Category: Veron M]] |
- | [[Category: Veron | + | |
- | + |
Current revision
ADENOSINE 5'-DIPHOSPHATE BINDING AND THE ACTIVE SITE OF NUCLEOSIDE DIPHOSPHATE KINASE
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