3f0t Summary

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Crystal structure of thymidine kinase from Herpes simplex virus type 1 in complex with N-methyl-DHBT

The structure was published by Martic, M., Pernot, L., Westermaier, Y., et al., Raic-Malic, S., Scapozza, L., and Ametamey, S., in 2011 in a paper entitled "Synthesis, crystal structure, and in vitro biological evaluation of C-6 pyrimidine derivatives: new lead structures for monitoring gene expression in vivo." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2008.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of Thymidine kinase.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Thymidine kinase P03176 (45-376) (KITH_HHV11)search Herpes simplex virus (type 1 / strain 17)search 91% 332 94%
B Thymidine kinase P03176 (45-376) (KITH_HHV11)search Herpes simplex virus (type 1 / strain 17)search 91% 332 94%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P03176 (45 - 376) Thymidine kinase Herpes simplex virus (type 1 / strain 17)

Chain Structural classification (CATH) Sequence family (Pfam)
A, B (P03176) P-loop containing nucleotide triphosphate hydrolasessearch PF00693: Thymidine kinase from herpesvirussearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (P03176) thymidine kinase activitysearch ATP bindingsearch TMP biosynthetic processsearch

Chain InterPro annotation
A, B Herpesvirus thymidine kinasesearch P-loop containing nucleoside triphosphate hydrolasesearch