5ukd

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{{STRUCTURE_5ukd| PDB=5ukd | SCENE= }}
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==PH INFLUENCES FLUORIDE COORDINATION NUMBER OF THE ALFX PHOSPHORYL TRANSFER TRANSITION STATE ANALOG==
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===PH INFLUENCES FLUORIDE COORDINATION NUMBER OF THE ALFX PHOSPHORYL TRANSFER TRANSITION STATE ANALOG===
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<StructureSection load='5ukd' size='340' side='right' caption='[[5ukd]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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==Function==
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<table><tr><td colspan='2'>[[5ukd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UKD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UKD FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AF3:ALUMINUM+FLUORIDE'>AF3</scene>, <scene name='pdbligand=C5P:CYTIDINE-5-MONOPHOSPHATE'>C5P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qf9|1qf9]], [[1ukd|1ukd]], [[2ukd|2ukd]], [[4ukd|4ukd]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KCY_DICDI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 ATCC 11735])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UMP/CMP_kinase UMP/CMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.14 2.7.4.14] </span></td></tr>
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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=5ukd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ukd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5ukd RCSB], [http://www.ebi.ac.uk/pdbsum/5ukd PDBsum]</span></td></tr>
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</table>
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== Function ==
[[http://www.uniprot.org/uniprot/KCY_DICDI KCY_DICDI]] This UMP-CMP kinase uses preferentially ATP as phosphate donor and is specific for UMP and CMP.
[[http://www.uniprot.org/uniprot/KCY_DICDI KCY_DICDI]] This UMP-CMP kinase uses preferentially ATP as phosphate donor and is specific for UMP and CMP.
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== Evolutionary Conservation ==
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==About this Structure==
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[[Image:Consurf_key_small.gif|200px|right]]
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[[5ukd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UKD OCA].
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Check<jmol>
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<jmolCheckbox>
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==Reference==
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uk/5ukd_consurf.spt"</scriptWhenChecked>
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<ref group="xtra">PMID:010426946</ref><references group="xtra"/><references/>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Atcc 11735]]
[[Category: Atcc 11735]]
[[Category: UMP/CMP kinase]]
[[Category: UMP/CMP kinase]]
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[[Category: Reinstein, J.]]
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[[Category: Reinstein, J]]
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[[Category: Schlichting, I.]]
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[[Category: Schlichting, I]]
[[Category: Nmp kinase]]
[[Category: Nmp kinase]]
[[Category: Nucleoside monophosphate kinase]]
[[Category: Nucleoside monophosphate kinase]]

Revision as of 10:59, 25 December 2014

PH INFLUENCES FLUORIDE COORDINATION NUMBER OF THE ALFX PHOSPHORYL TRANSFER TRANSITION STATE ANALOG

5ukd, resolution 1.90Å

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