1e9f
From Proteopedia
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==Mutant human thymidylate kinase complexed with TMP and ADP== | ==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 with sequence from [ | + | <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> |
- | </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]] 1.9Å</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>, <scene name='pdbligand=TMP:THYMIDINE-5-PHOSPHATE'>TMP</scene></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> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [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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==See Also== | ==See Also== | ||
- | *[[Thymidylate kinase|Thymidylate kinase]] | + | *[[Thymidylate kinase 3D structures|Thymidylate kinase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Escherichia coli]] |
- | [[Category: | + | [[Category: Homo sapiens]] |
- | [[Category: Brundiers | + | [[Category: Large Structures]] |
- | [[Category: Goody | + | [[Category: Brundiers R]] |
- | [[Category: Konrad | + | [[Category: Goody RS]] |
- | [[Category: Lavie | + | [[Category: Konrad M]] |
- | [[Category: Ostermann | + | [[Category: Lavie A]] |
- | [[Category: Padiyar | + | [[Category: Ostermann N]] |
- | [[Category: Reinstein | + | [[Category: Padiyar S]] |
- | [[Category: Schlichting | + | [[Category: Reinstein J]] |
- | [[Category: Veit | + | [[Category: Schlichting I]] |
- | + | [[Category: Veit T]] | |
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Current revision
Mutant human thymidylate kinase complexed with TMP and ADP
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Categories: Escherichia coli | Homo sapiens | Large Structures | Brundiers R | Goody RS | Konrad M | Lavie A | Ostermann N | Padiyar S | Reinstein J | Schlichting I | Veit T