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1e9a
From Proteopedia
(Difference between revisions)
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<StructureSection load='1e9a' size='340' side='right'caption='[[1e9a]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1e9a' size='340' side='right'caption='[[1e9a]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1e9a]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1e9a]] 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=1E9A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E9A FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=Z5A:P1-(5-ADENOSYL)P5-(5-(3AZIDO-3-DEOXYTHYMIDYL))PENTAPHOSPHATE'>Z5A</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=Z5A:P1-(5-ADENOSYL)P5-(5-(3AZIDO-3-DEOXYTHYMIDYL))PENTAPHOSPHATE'>Z5A</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]], [[1e9b|1e9b]], [[1e9c|1e9c]], [[1e9d|1e9d]], [[1e9e|1e9e]], [[1e9f|1e9f]]</td></tr> | + | <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]], [[1e9b|1e9b]], [[1e9c|1e9c]], [[1e9d|1e9d]], [[1e9e|1e9e]], [[1e9f|1e9f]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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> |
| - | <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=1e9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e9a OCA], [https://pdbe.org/1e9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e9a RCSB], [https://www.ebi.ac.uk/pdbsum/1e9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e9a ProSAT]</span></td></tr> |
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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==See Also== | ==See Also== | ||
| - | *[[Thymidylate kinase|Thymidylate kinase]] | + | *[[Thymidylate kinase 3D structures|Thymidylate kinase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 05:46, 28 April 2021
Human thymidylate kinase complexed with the bisubstrate inhibitor AZTP5A
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Categories: Human | Large Structures | DTMP kinase | Brundiers, R | Goody, R S | Konrad, M | Lavie, A | Ostermann, N | Padiyar, S | Reintein, J | Schlichting, I | Veit, T | P-loop | Phosphotransferase | Thymidylate kinase | Transferase

