1e98
From Proteopedia
(Difference between revisions)
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- | [[Image:1e98.png|left|200px]] | ||
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{{STRUCTURE_1e98| PDB=1e98 | SCENE= }} | {{STRUCTURE_1e98| PDB=1e98 | SCENE= }} | ||
+ | ===Wild type human thymidylate kinase complexed with AZTMP and ADP=== | ||
+ | {{ABSTRACT_PUBMED_11071809}} | ||
- | === | + | ==Function== |
- | + | [[http://www.uniprot.org/uniprot/KTHY_HUMAN KTHY_HUMAN]] Catalyzes the conversion of dTMP to dTDP. | |
- | + | ||
==About this Structure== | ==About this Structure== | ||
[[1e98]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E98 OCA]. | [[1e98]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E98 OCA]. | ||
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+ | ==See Also== | ||
+ | *[[Thymidylate kinase|Thymidylate kinase]] | ||
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID:011071809</ref><references group="xtra"/> | + | <ref group="xtra">PMID:011071809</ref><ref group="xtra">PMID:010873853</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: DTMP kinase]] | [[Category: DTMP kinase]] | ||
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[[Category: P-loop]] | [[Category: P-loop]] | ||
[[Category: Phosphotransferase]] | [[Category: Phosphotransferase]] | ||
- | [[Category: | + | [[Category: Transferase]] |
Revision as of 06:22, 16 May 2013
Contents |
Wild type human thymidylate kinase complexed with AZTMP and ADP
Template:ABSTRACT PUBMED 11071809
Function
[KTHY_HUMAN] Catalyzes the conversion of dTMP to dTDP.
About this Structure
1e98 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Ostermann N, Lavie A, Padiyar S, Brundiers R, Veit T, Reinstein J, Goody RS, Konrad M, Schlichting I. Potentiating AZT activation: structures of wild-type and mutant human thymidylate kinase suggest reasons for the mutants' improved kinetics with the HIV prodrug metabolite AZTMP. J Mol Biol. 2000 Nov 17;304(1):43-53. PMID:11071809 doi:10.1006/jmbi.2000.4175
- Ostermann N, Schlichting I, Brundiers R, Konrad M, Reinstein J, Veit T, Goody RS, Lavie A. Insights into the phosphoryltransfer mechanism of human thymidylate kinase gained from crystal structures of enzyme complexes along the reaction coordinate. Structure. 2000 Jun 15;8(6):629-42. PMID:10873853