1e9f

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<StructureSection load='1e9f' size='340' side='right'caption='[[1e9f]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1e9f' size='340' side='right'caption='[[1e9f]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1e9f]] is a 1 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=1E9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E9F FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1e9f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1E9F FirstGlance]. <br>
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</td></tr><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>, <scene name='pdbligand=TMP:THYMIDINE-5-PHOSPHATE'>TMP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1e2d|1e2d]], [[1e2e|1e2e]], [[1e2f|1e2f]], [[1e2g|1e2g]], [[1e2q|1e2q]], [[1e98|1e98]], [[1e99|1e99]], [[1e9a|1e9a]], [[1e9b|1e9b]], [[1e9c|1e9c]], [[1e9d|1e9d]], [[1e9e|1e9e]]</div></td></tr>
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<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>, <scene name='pdbligand=TMP:THYMIDINE-5-PHOSPHATE'>TMP</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e9f OCA], [https://pdbe.org/1e9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e9f RCSB], [https://www.ebi.ac.uk/pdbsum/1e9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e9f ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e9f OCA], [https://pdbe.org/1e9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e9f RCSB], [https://www.ebi.ac.uk/pdbsum/1e9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e9f ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/KTHY_HUMAN KTHY_HUMAN]] Catalyzes the conversion of dTMP to dTDP.
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[https://www.uniprot.org/uniprot/KTHY_HUMAN KTHY_HUMAN] Catalyzes the conversion of dTMP to dTDP.[https://www.uniprot.org/uniprot/KTHY_ECOLI KTHY_ECOLI] Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Escherichia coli]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: DTMP kinase]]
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[[Category: Brundiers R]]
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[[Category: Brundiers, R]]
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[[Category: Goody RS]]
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[[Category: Goody, R S]]
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[[Category: Konrad M]]
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[[Category: Konrad, M]]
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[[Category: Lavie A]]
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[[Category: Lavie, A]]
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[[Category: Ostermann N]]
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[[Category: Ostermann, N]]
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[[Category: Padiyar S]]
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[[Category: Padiyar, S]]
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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]]
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[[Category: Veit T]]
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[[Category: Veit, T]]
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[[Category: P-loop]]
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[[Category: Phosphotransferase]]
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[[Category: Thymidylate kinase]]
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[[Category: Transferase]]
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Current revision

Mutant human thymidylate kinase complexed with TMP and ADP

PDB ID 1e9f

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