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1e9f
From Proteopedia
(Difference between revisions)
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| - | == | + | |
| + | ==Mutant human thymidylate kinase complexed with TMP and ADP== | ||
<StructureSection load='1e9f' size='340' side='right' caption='[[1e9f]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1e9f' size='340' side='right' caption='[[1e9f]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1e9f]] is a 1 chain structure | + | <table><tr><td colspan='2'>[[1e9f]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E9F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E9F FirstGlance]. <br> |
</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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TMP:THYMIDINE-5-PHOSPHATE'>TMP</scene></td></tr> | </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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TMP:THYMIDINE-5-PHOSPHATE'>TMP</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e2d|1e2d]], [[1e2e|1e2e]], [[1e2f|1e2f]], [[1e2g|1e2g]], [[1e2q|1e2q]], [[1e98|1e98]], [[1e99|1e99]], [[1e9a|1e9a]], [[1e9b|1e9b]], [[1e9c|1e9c]], [[1e9d|1e9d]], [[1e9e|1e9e]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e2d|1e2d]], [[1e2e|1e2e]], [[1e2f|1e2f]], [[1e2g|1e2g]], [[1e2q|1e2q]], [[1e98|1e98]], [[1e99|1e99]], [[1e9a|1e9a]], [[1e9b|1e9b]], [[1e9c|1e9c]], [[1e9d|1e9d]], [[1e9e|1e9e]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </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=1e9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e9f OCA], [http://pdbe.org/1e9f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e9f RCSB], [http://www.ebi.ac.uk/pdbsum/1e9f 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=1e9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e9f OCA], [http://pdbe.org/1e9f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e9f RCSB], [http://www.ebi.ac.uk/pdbsum/1e9f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e9f ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/KTHY_HUMAN KTHY_HUMAN]] Catalyzes the conversion of dTMP to dTDP. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </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/ | + | </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=1e9f ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Human]] | ||
[[Category: DTMP kinase]] | [[Category: DTMP kinase]] | ||
[[Category: Brundiers, R]] | [[Category: Brundiers, R]] | ||
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[[Category: Phosphotransferase]] | [[Category: Phosphotransferase]] | ||
[[Category: Thymidylate kinase]] | [[Category: Thymidylate kinase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 13:24, 15 March 2017
Mutant human thymidylate kinase complexed with TMP and ADP
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