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Showing drug card for Vidarabine (DB00194)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:04:41
Primary Accession Number DB00194
Secondary Accession Number
  • APRD00333
  • EXPT02753
Name Vidarabine
Drug Type
  • Approved
  • Small Molecule
Description A nucleoside antibiotic isolated from Streptomyces antibioticus. It has some antineoplastic properties and has broad spectrum activity against DNA viruses in cell cultures and significant antiviral activity against infections caused by a variety of viruses such as the herpes viruses, the vaccinia VIRUS and varicella zoster virus. [PubChem]
Synonyms
  1. 9-beta-D-arabinofuranosyl-adenine
  2. Adenine Arabinoside
  3. Ara Atp
  4. Ara-A
  5. Ara-Atp
  6. Ara-a Triphosphate
  7. Araadenosine
  8. Arabinofuranosyladenine Triphosphate
  9. Arabinoside Adenine
  10. Arabinosyl Adenine
  11. Arabinosyl-Atp
  12. Arabinosyladenine
  13. Arabinosyladenine Triphosphate
  14. Vidarabine Triphosphate
Brand Names
  1. Arasena-A
  2. Spongoadenosine
  3. Vidarabin
  4. Vira-A
Brand Mixtures Not Available
Chemical IUPAC Name (2R,3S,4S,5R)-2-(6-aminopurin-9-yl)-5-(hydroxymethyl)oxolane-3,4-diol hydrate
Chemical Formula C10H15N5O5
Chemical Structure Structure
CAS Registry Number 24356-66-9
InChI Identifier InChI=1/C10H13N5O4.H2O/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(18)6(17)4(1-16)19-10;/h2-4,6-7,10,16-18H,1H2,(H2,11,12,13);1H2/t4-,6-,7+,10-;/m1./s1/f/h11H2;
InChI Key ZTHWFVSEMLMLKT-QGDLRDFBDG
KEGG Drug D00406 Link Image
KEGG Compound C07195 Link Image
PubChem Compound 32326 Link Image
PubChem Substance 174304 Link Image
ChEBI ID Not Available
PharmGKB ID PA451876 Link Image
HET ID RAB Link Image
GenBank ID Not Available
Drug ID Number [DIN] Not Available
RxList Link http://www.rxlist.com/cgi/generic3/vidarabine.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Vidarabine Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 285.2566
Monoisotopic Molecular Weight 285.1073
State Solid
Melting Point Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility Not Available Calculated using ALOGPS
Experimental LogP/Hydrophobicity -2.115 Source: PhysProp
Predicted LogP Not Available Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS Not Available Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID 1PW7 Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES O.NC1=C2N=CN([C@@H]3O[C@H](CO)[C@@H](O)[C@@H]3O)C2=NC=N1
Canonical SMILES O.NC1=C2N=CN(C3OC(CO)C(O)C3O)C2=NC=N1
Drug Category
  • Antimetabolites
  • Antiviral Agents
ATC Codes
AHFS Codes Not Available
Indication For treatment of chickenpox - varicella, herpes zoster and herpes simplex
Pharmacology Vidarabine is a synthetic purine nucleoside analogue with in vitro and in vivo inhibitory activity against herpes simplex virus types 1 (HSV-1), 2 (HSV-2), and varicella-zoster virus (VZV). The inhibitory activity of Vidarabine is highly selective due to its affinity for the enzyme thymidine kinase (TK) encoded by HSV and VZV. This viral enzyme converts Vidarabine into Vidarabine monophosphate, a nucleotide analogue. The monophosphate is further converted into diphosphate by cellular guanylate kinase and into triphosphate by a number of cellular enzymes. in vitro, Vidarabine triphosphate stops replication of herpes viral DNA. When used as a substrate for viral DNA polymerase, Vidarabine triphosphate competitively inhibits dATP leading to the formation of 'faulty' DNA. This is where Vidarabine triphosphate is incorporated into the DNA strand replacing many of the adenosine bases. This results in the prevention of DNA synthesis, as phosphodiester bridges can longer to be built, destabilizing the strand.
Mechanism of Action Vidarabine stops replication of herpes viral DNA in 3 ways: 1) competitive inhibition of viral DNA polymerase, 2) incorporation into and termination of the growing viral DNA chain, and 3) inactivation of the viral DNA polymerase.
Absorption Systemetic absorption of vidarabine should not be expected to occur following ocular administration and swallowing lacrimal secretions.
Toxicity Acute massive overdosage by oral ingestion of the ophthalmic ointment has not occurred. However, the rapid deamination to arabinosylhypoxanthine should preclude any difficulty. The oral LD50 for vidarabine is greater than 5020 mg/kg in mice and rats. No untoward effects should result from ingestion of the entire contents of the tube. Overdosage by ocular instillation is unlikely because any excess should be quickly expelled from the conjunctival sac.
Protein Binding 24-38%
Biotransformation In laboratory animals, vidarabine is rapidly deaminated in the gastrointestinal tract to Ara-Hx.
Half Life Not Available
Dosage Forms
Form Route
Ointment Ophthalmic
Patient Information Not Available
Contraindications Show Link Image
Interactions Not Available
Drug Interactions Not Available
Food Interactions Not Available
Pathways Not Available
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
Organisms Affected
  • Human Herpes Virus
Phase 1 Metabolizing Enzymes
  1. Adenosine deaminase
Targets
  1. Thymidine kinase
  2. DNA
  3. Purine nucleoside phosphorylase deoD-type
  4. DNA polymerase
  5. Thymidine kinase
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Adenosine deaminase
Enzyme 1 Gene Name ADA
Enzyme 1 SwissProt ID P00813 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >Adenosine deaminase 
AQTPAFDKPKVELHVHLDGSIKPETILYYGRRRGIALPANTAEGLLNVIGMDKPLTLPDF
LAKFDYYMPAIAGCREAIKRIAYEFVEMKAKEGVVYVEVRYSPHLLANSKVEPIPWNQAE
GDLTPDEVVALVGQGLQEGERDFGVKARSILCCMRHQPNWSPKVVELCKKYQQQTVVAID
LAGDETIPGSSLLPGHVQAYQEAVKSGIHRTVHAGEVGSAEVVKEAVDILKTERLGHGYH
TLEDQALYNRLRQENMHFEICPWSSYLTGAWKPDTEHAVIRLKNDQANYSLNTDDPLIFK
STLDTDYQMTKRDMGFTEEEFKRLNINAAKSSFLPEDEKRELLDLLYKAYGMPPSASAGQ
NL
Drug Target 1 [top]
Target 1 ID 509
Target 1 Name Thymidine kinase
Target 1 Synonyms
  1. EC 2.7.1.21
Target 1 Gene Name TK
Target 1 Protein Sequence >Thymidine kinase 
MASYPCHQHASAFDQAARSRGHSNRRTALRPRRQQEATEVRLEQKMPTLLRVYIDGPHGM
GKTTTTQLLVALGSRDDIVYVPEPMTYWQVLGASETIANIYTTQHRLDQGEISAGDAAVV
MTSAQITMGMPYAVTDAVLAPHIGGEAGSSHAPPPALTLIFDRHPIAALLCYPAARYLMG
SMTPQAVLAFVALIPPTLPGTNIVLGALPEDRHIDRLAKRQRPGERLDLAMLAAIRRVYG
LLANTVRYLQGGGSWREDWGQLSGTAVPPQGAEPQSNAGPRPHIGDTLFTLFRAPELLAP
NGDLYNVFAWALDVLAKRLRPMHVFILDYDQSPAGCRDALLQLTSGMVQTHVTTPGSIPT
ICDLARTFAREMGEAN
Target 1 Number of Residues 382
Target 1 Molecular Weight 40897
Target 1 Theoretical pI 7.70
Target 1 GO Classification
Function
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
kinase activity
nucleobase, nucleoside, nucleotide kinase activity
nucleoside kinase activity
deoxynucleoside kinase activity
thymidine kinase activity
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
nucleotide metabolism
pyrimidine nucleotide metabolism
pyrimidine nucleotide biosynthesis
pyrimidine nucleoside monophosphate biosynthesis
pyrimidine ribonucleoside monophosphate biosynthesis
TMP biosynthesis
Component
Not Available
Target 1 General Function Involved in thymidine kinase activity
Target 1 Specific Function In latent infection, may allow the virus to be reactivated and to grow in cells lacking a high concentration of phosphorylated nucleic acid precursors, such as nerve cells that do not replicate their genome
Target 1 Pathways
Name SMPDB Link KEGG Link
Pyrimidine metabolism SMP00046 Link Image map00240 Link Image
Target 1 Reactions
  • ATP + thymidine = ADP + thymidine 5'-phosphate
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 8100965 Link Image
Target 1 UniProtKB/Swiss-Prot ID Q9QNF7 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name KITH_HHV1 Link Image
Target 1 PDB ID 1OF1 Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location Not Available
Target 1 Gene Sequence >1131 bp 
ATGGCTTCGTACCCCTGCCATCAACACGCGTCTGCGTTCGACCAGGCTGCGCGTTCTCGC
GGCCATAGCAACCGACGTACGGCGTTGCGCCCTCGCCGGCAGCAAGAAGCCACGGAAGTC
CGCCTGGAGCAGAAAATGCCCACGCTACTGCGGGTTTATATAGACGGTCCTCACGGGATG
GGGAAAACCACCACCACGCAACTGCTGGTGGCCCTGGGTTCGCGCGACGATATCGTCTAC
GTACCCGAGCCGATGACTTACTGGCAGGTGCTGGGGGCTTCCGAGACAATCGCGAACATC
TACACCACACAACACCGCCTCGACCAGGGTGAGATATCGGCCGGGGACGCGGCGGTGGTA
ATGACAAGCGCCCAGATAACAATGGGCATGCCTTATGCCGTGACCGACGCCGTTCTGGCT
CCTCATATCGGGGGGGAGGCTGGGAGCTCACATGCCCCGCCCCCGGCCCTCACCCTCATC
TTCGACCGCCATCCCATCGCCGCCCTCCTGTGCTACCCGGCCGCGCGATACCTTATGGGC
AGCATGACCCCCCAGGCCGTGCTGGCGTTCGTGGCCCTCATCCCGCCGACCTTGCCCGGC
ACAAACATCGTGTTGGGGGCCCTTCCGGAGGACAGACACATCGACCGCCTGGCCAAACGC
CAGCGCCCCGGCGAGCGGCTTGACCTGGCTATGCTGGCCGCGATTCGCCGCGTTTACGGG
CTGCTTGCCAATACGGTGCGGTATCTGCAGGGCGGCGGGTCGTGGCGGGAGGATTGGGGA
CAGCTTTCGGGGACGGCCGTGCCGCCCCAGGGTGCCGAGCCCCAGAGCAACGCGGGCCCA
CGACCCCATATCGGGGACACGTTATTTACCCTGTTTCGGGCCCCCGAGTTGCTGGCCCCC
AACGGCGACCTGTATAACGTGTTTGCCTGGGCCTTGGACGTCTTGGCCAAACGCCTCCGT
CCCATGCACGTCTTTATCCTGGATTACGACCAATCGCCCGCCGGCTGCCGGGACGCCCTG
CTGCAACTTACCTCCGGGATGGTCCAGACCCACGTCACCACCCCAGGCTCCATACCGACG
ATCTGCGACCTGGCGCGCACGTTTGCCCGGGAGATGGGGGAGGCTAACTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID Not Available
Target 1 GenAtlas ID Not Available
Target 1 HGNC ID Not Available
Target 1 Chromosome Location MT
Target 1 Locus -
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Nagamine M, Suzutani T, Saijo M, Hayashi K, Azuma M: Comparison of polymorphism of thymidine kinase gene and restriction fragment length polymorphism of genomic DNA in herpes simplex virus type 1. J Clin Microbiol. 2000 Jul;38(7):2750-2. [PubMed Link Image]
  2. Morfin F, Souillet G, Bilger K, Ooka T, Aymard M, Thouvenot D: Genetic characterization of thymidine kinase from acyclovir-resistant and -susceptible herpes simplex virus type 1 isolated from bone marrow transplant recipients. J Infect Dis. 2000 Jul;182(1):290-3. Epub 2000 Jun 19. [PubMed Link Image]
Target 1 Drug References
  1. Henrot A: [Mother-infant and indirect transmission of HSV infection: treatment and prevention] Ann Dermatol Venereol. 2002 Apr;129(4 Pt 2):533-49. [PubMed Link Image]
  2. Suzuki M, Okuda T, Shiraki K: Synergistic antiviral activity of acyclovir and vidarabine against herpes simplex virus types 1 and 2 and varicella-zoster virus. Antiviral Res. 2006 Nov;72(2):157-61. Epub 2006 May 30. [PubMed Link Image]
  3. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  4. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 874
Target 2 Name DNA
Target 2 Synonyms
  1. Deoxyribonucleic acid
Target 2 Gene Name Not Available
Target 2 Protein Sequence Not Available
Target 2 Number of Residues 0
Target 2 Molecular Weight 7656 (double strand)
Target 2 Theoretical pI Not Available
Target 2 GO Classification
Function
information storage
information transfer
Process
DNA replication and chromosomal cycle
DNA replication
DNA-dependent DNA replication
DNA replication, synthesis of RNA primer
transcription
transcription, DNA dependent
Component
cell
intracellular
nucleus
mitochondria
Target 2 General Function Biological information storage and information transfer
Target 2 Specific Function DNA is the molecule of heredity, as it is responsible for the genetic propagation of most inherited traits. It is a polynucleic acid that carries genetic information on cell growth, division, and function. DNA consists of two long strands of nucleotides twisted into a double helix and held together by hydrogen bonds. The sequence of nucleotides determines hereditary characteristics. Each strand serves as the template for subsequent DNA replication and as a template for mRNA production, leading to protein synthesis via ribosomes.
Target 2 Pathways
Name SMPDB Link KEGG Link
DNA polymerase map03030 Link Image
RNA polymerase map03020 Link Image
Target 2 Reactions
  • DNA + DNA polymerase + nNTP = 2 DNA + nNDP; DNA + RNA polymerase + NTP = mRNA + nNDP
Target 2 Pfam Domain Function Not Available
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Essential
Target 2 GenBank ID Protein Not Available
Target 2 UniProtKB/Swiss-Prot ID Not Available
Target 2 UniProtKB/Swiss-Prot Entry Name Not Available
Target 2 PDB ID 1BNA Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Nucleus and mitochondria
Target 2 Gene Sequence >Example: Dickerson dodecamer 
CGCGAATTCGCG
Target 2 GenBank Gene ID
Target 2 GeneCard ID Not Available
Target 2 GenAtlas ID Not Available
Target 2 HGNC ID Not Available
Target 2 Chromosome Location Not Available
Target 2 Locus All loci
Target 2 SNPs Not Available
Target 2 General References
  1. Nadeau D, Marchand C: Change in the kinetics of sulphacetamide tissue distribution in Walker tumor-bearing rats. Drug Metab Dispos. 1975 Nov-Dec;3(6):565-76. [PubMed Link Image]
Target 2 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 3683
Target 3 Name Purine nucleoside phosphorylase deoD-type
Target 3 Synonyms
  1. EC 2.4.2.1
  2. Inosine phosphorylase
  3. PNP
Target 3 Gene Name deoD
Target 3 Protein Sequence >Purine nucleoside phosphorylase deoD-type 
MATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISV
MGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIR
FKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFYSPDGEMFDVMEKYGILGVE
MEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDKE
Target 3 Number of Residues 242
Target 3 Molecular Weight 25950
Target 3 Theoretical pI 5.35
Target 3 GO Classification
Function
catalytic activity
transferase activity
transferase activity, transferring glycosyl groups
transferase activity, transferring pentosyl groups
purine-nucleoside phosphorylase activity
Process
nucleoside metabolism
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
Component
Not Available
Target 3 General Function Nucleotide transport and metabolism
Target 3 Specific Function Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules
Target 3 Pathways
Name SMPDB Link KEGG Link
Purine metabolism SMP00050 Link Image map00230 Link Image
Target 3 Reactions
  • purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 147309 Link Image
Target 3 UniProtKB/Swiss-Prot ID P0ABP8 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name DEOD_ECOLI Link Image
Target 3 PDB ID 1PW7 Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location Not Available
Target 3 Gene Sequence >720 bp 
ATGGCTACCCCACACATTAATGCAGAAATGGGCGATTTCGCTGACGTAGTTTTGATGCCA
GGCGACCCGCTGCGTGCGAAGTATATTGCTGAAACTTTCCTTGAAGATGCCCGTGAAGTG
AACAACGTTCGCGGTATGCTGGGCTTCACCGGTACTTACAAAGGCCGCAAAATTTCCGTA
ATGGGTCACGGTATGGGTATCCCGTCCTGCTCCATCTACACCAAAGAACTGATCACCGAT
TTCGGCGTGAAGAAAATTATCCGCGTGGGTTCCTGTGGCGCAGTTCTGCCGCACGTAAAA
CTGCGCGACGTCGTTATCGGTATGGGTGCCTGCACCGATTCCAAAGTTAACCGCATCCGT
TTTAAAGACCATGACTTTGCCGCTATCGCTGACTTCGACATGGTGCGTAACGCAGTAGAT
GCAGCTAAAGCACTGGGTATTGATGCTCGCGTGGGTAACCTGTTCTCCGCTGACCTGTTC
TACTCTCCGGACGGCGAAATGTTCGACGTGATGGAAAAATACGGCATTCTCGGCGTGGAA
ATGGAAGCGGCTGGTATCTACGGCGTCGCTGCAGAATTTGGCGCGAAAGCCCTGACCATC
TGCACCGTATCTGACCACATCCGCACTCACGAGCAGACCACTGCCGCTGAGCGTCAGACT
ACCTTCAACGACATGATCAAAATCGCACTGGAATCCGTTCTGCTGGGCGATAAAGAGTAA
Target 3 GenBank Gene ID
Target 3 GeneCard ID Not Available
Target 3 GenAtlas ID Not Available
Target 3 HGNC ID Not Available
Target 3 Chromosome Location Not Available
Target 3 Locus Not Available
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Hershfield MS, Chaffee S, Koro-Johnson L, Mary A, Smith AA, Short SA: Use of site-directed mutagenesis to enhance the epitope-shielding effect of covalent modification of proteins with polyethylene glycol. Proc Natl Acad Sci U S A. 1991 Aug 15;88(16):7185-9. [PubMed Link Image]
  2. Larsen JE, Albrechtsen B, Valentin-Hansen P: Analysis of the terminator region after the deoCABD operon of Escherichia coli K-12 using a new class of single copy number operon-fusion vectors. Nucleic Acids Res. 1987 Jul 10;15(13):5125-40. [PubMed Link Image]
  3. Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. [PubMed Link Image]
  4. Henzel WJ, Billeci TM, Stults JT, Wong SC, Grimley C, Watanabe C: Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5011-5. [PubMed Link Image]
  5. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
  6. Mao C, Cook WJ, Zhou M, Koszalka GW, Krenitsky TA, Ealick SE: The crystal structure of Escherichia coli purine nucleoside phosphorylase: a comparison with the human enzyme reveals a conserved topology. Structure. 1997 Oct 15;5(10):1373-83. [PubMed Link Image]
  7. Koellner G, Luic M, Shugar D, Saenger W, Bzowska A: Crystal structure of the ternary complex of E. coli purine nucleoside phosphorylase with formycin B, a structural analogue of the substrate inosine, and phosphate (Sulphate) at 2.1 A resolution. J Mol Biol. 1998 Jul 3;280(1):153-66. [PubMed Link Image]
Target 3 Drug References Not Available
Drug Target 4 [top]
Target 4 ID 4104
Target 4 Name DNA polymerase
Target 4 Synonyms
  1. EC 2.7.7.7
Target 4 Gene Name Not Available
Target 4 Protein Sequence >DNA polymerase 
MSGGLFYNPFLRPNKGLLKKPDKEYLRLIPKCFQTPGAAGVVDVRGPQPPLCFYQDSLTV
VGGDEDGKGMWWRQRAQEGTARPEADTHGSPLDFHVYDILETVYTHEKCAVIPSDKQGYV
VPCGIVIKLLGRRKADGASVCVNVFGQQAYFYASAPQGLDVEFAVLSALKASTFDRRTPC
RVSVEKVTRRSIMGYGNHAGDYHKITLSHPNSVCHVATWLQDKHGCRIFEANVDATRRFV
LDNDFVTFGWYSCRRAIPRLQHRDSYAELEYDCEVGDLSVRREDSSWPSYQALAFDIECL
GEEGFPTATNEADLILQISCVLWSTGEEAGRYRRILLTLGTCEDIEGVEVYEFPSELDML
YAFFQLIRDLSVEIVTGYNVANFDWPYILDRARHIYSINPASLGKIRAGGVCEVRRPHDA
GKGFLRANTKVRITGLIPIDMYAVCRDKLSLSDYKLDTVARHLLGAKKEDVHYKEIPRLF
AAGPEGRRRLGMYCVQDSALVMDLLNHFVIHVEVAEIAKIAHIPCRRVLDDGQQIRVFSC
LLAAAQKENFILPMPSASDRDGYQGATVIQPLSGFYNSPVLVVDFASLYPSIIQAHNLCY
STMITPGEEHRLAGLRPGEDYESFRLTGGVYHFVKKHVHESFLASLLTSWLAKRKAIKKL
LAACEDPRQRTILDKQQLAIKCTCNAVYGFTGVANGLFPCLSIAETVTLQGRTMLERAKA
FVEALSPANLQALAPSPDAWAPLNPEGQLRVIYGDTDSLFIECRGFSESETLRFADALAA
HTTRSLFVAPISLEAEKTFSCLMLITKKRYVGVLTDGKTLMKGVELVRKTACKFVQTRCR
RVLDLVLADARVKEAASLLSHRPFQESFTQGLPVGFLPVIDILNQAYTDLREGRVPMGEL
CFSTELSRKLSAYKSTQMPHLAVYQKFVERNEELPQIHDRIQYVFVEPKGGVKGARKTEM
AEDPAYAERHGVPVAVDHYFDKLLQGAANILQCLFDNNSGAALSVLQNFTARPPF
Target 4 Number of Residues 1031
Target 4 Molecular Weight 113419
Target 4 Theoretical pI 7.47
Target 4 GO Classification
Function
hydrolase activity
hydrolase activity, acting on ester bonds
nuclease activity
exonuclease activity
3'-5' exonuclease activity
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
nucleotidyltransferase activity
DNA-directed DNA polymerase activity
nucleic acid binding
DNA binding
binding
nucleotide binding
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
DNA metabolism
DNA replication
Component
Not Available
Target 4 General Function Replication, recombination and repair
Target 4 Specific Function Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Target 4 Pathways
Name SMPDB Link KEGG Link
DNA polymerase map00230 Link Image
Target 4 Reactions
  • deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Essential
Target 4 GenBank ID Protein 1334913 Link Image
Target 4 UniProtKB/Swiss-Prot ID P03198 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name DPOL_EBV Link Image
Target 4 PDB ID Not Available
Target 4 Cellular Location
  • Nucleus
Target 4 Gene Sequence >3048 bp 
TTAGAATGGTGGCCGGGCTGTAAAATTCTGGAGGACGGAGAGGGCGGCCCCGGAGTTGTT
ATCAAAGAGGCACTGGAGGATGTTGGCCGCTCCTTGGAGCAGCTTGTCGAAATAATGATC
CACGGCCACGGGAACGCCGTGCCGCTCGGCGTAGGCCGGGTCCTCGGCCATCTCCGTCTT
TCTCGCCCCCTTCACTCCCCCCTTGGGCTCCACAAAGACGTACTGGATGCGGTCGTGGAT
CTGGGGCAGTTCCTCGTTGCGCTCGACGAACTTCTGGTAGACGGCCAGGTGAGGCATCTG
GGTGCTCTTGTAGGCTGAGAGCTTGCGGCTGAGCTCCGTTGAAAAGCAGAGCTCCCCCAT
GGGGACCCTGCCTTCACGGAGGTCTGTGTAGGCCTGGTTTAGGATGTCAATGACGGGCAA
AAAGCCCACAGGTAGCCCTTGTGTAAATGACTCTTGGAAGGGCCGGTGGGAGAGGAGGCT
GGCCGCCTCCTTTACCCGGGCATCCGCCAGCACCAGGTCGAGCACGCGCCGGCAGCGTGT
CTGCACAAACTTGCAGGCCGTCTTCCGGACGAGCTCCACCCCCTTCATCAGGGTCTTGCC
GTCCGTCAGCACCCCCACATATCTCTTCTTTGTAATCAGCATCAGGCAGGAGAAGGTCTT
CTCGGCCTCCAGGGAGATGGGGGCCACAAACAGGCTCCGGGTGGTGTGGGCGGCCAGGGC
ATCGGCAAAGCGCAGGGTCTCGCTCTCTGAAAACCCCCGGCACTCGATAAACAGCGAGTC
CGTGTCCCCGTAGATGACTCGAAGCTGGCCCTCGGGGTTGAGGGGCGCCCAGGCGTCCGG
GGAGGGGGCCAGGGCCTGCAGGTTGGCGGGGCTCAGGGCCTCCACGAAGGCCTTGGCCCG
CTCCAACATCGTGCGGCCCTGCAGCGTCACCGTCTCGGCGATGGAGAGGCAGGGAAAGAG
GCCGTTGGCCACCCCGGTGAAGCCGTAGACGGCGTTGCACGTGCACTTGATGGCCAGCTG
CTGCTTGTCGAGGATGGTCCTTTGGCGCGGATCCTCGCAGGCCGCCAGCAGCTTCTTGAT
GGCCTTGCGCTTGGCCAGCCAGGAGGTCAACAGACTAGCCAAGAAGGACTCGTGCACGTG
CTTCTTTACAAAGTGGTAGACGCCCCCCGTGAGCCTGAAGGACTCATAGTCTTCTCCCGG
GCGCAGGCCGGCTAGCCTGTGCTCTTCTCCCGGCGTTATCATGGTAGAATAACAGAGATT
ATGAGCCTGAATGATGCTCGGGTAGAGGCTGGCAAAGTCCACCACCAGAACCGGGGAGTT
GTAGAATCCGGACAGGGGCTGGATGACGGTGGCCCCCTGGTAGCCGTCCCGGTCAGAGGC
CGAGGGCATGGGCAGGATAAAGTTTTCCTTTTGGGCGGCCGCCAGGAGGCAGGAGAACAC
GCGGATCTGCTGCCCATCGTCCAGCACCCGCCTGCAGGGGATGTGAGCGATCTTGGCAAT
CTCTGCCACCTCCACGTGGATCACGAAATGGTTTAGCAGATCCATGACCAGGGCCGAGTC
CTGCACGCAGTACATGCCGAGCCGCCTGCGCCCCTCGGGGCCCGCTGCAAAGAGGCGAGG
AATCTCCTTGTAATGCACATCCTCCTTCTTGGCCCCCAGTAGGTGCCTGGCTACTGTGTC
CAGCTTGTAGTCTGAGAGGCTGAGCTTGTCCCGGCACACGGCGTACATGTCGATGGGGAT
GAGGCCGGTGATGCGGACCTTGGTGTTGGCCCGCAAGAAGCCCTTGCCCGCATCATGGGG
TCGCCTGACCTCGCAGACGCCCCCAGCCCTAATTTTGCCCAGAGAGGCTGGGTTGATGCT
GTAGATGTGCCTGGCTCTGTCCAGAATGTAGGGCCAGTCAAAGTTGGCCACGTTGTAGCC
GGTCACAATCTCCACGCTGAGGTCTCTGATGAGCTGGAAGAAGGCGTAGAGCATGTCCAG
CTCCGATGGGAACTCGTAGACCTCAACCCCCTCTATGTCTTCGCAGGTGCCCAGCGTCAG
CAGGATGCGCCTATAGCGCCCGGCCTCCTCCCCTGTCGACCAGAGGACGCAGGATATCTG
CAGGATCAGGTCAGCCTCGTTGGTGGCCGTGGGGAAGCCCTCCTCCCCCAGACACTCGAT
ATCGAAGGCCAGGGCCTGGTAGGAGGGCCAGGAGCTGTCTTCACGCCGGACCGAGAGGTC
GCCCACCTCACAGTCGTACTCGAGCTCGGCGTACGAGTCCCGGTGCTGGAGGCGGGGGAT
GGCGCGGCGGCAGCTGTACCAGCCAAAGGTGACAAAGTCATTGTCCAGGACAAAGCGGCG
CGTGGCATCCACGTTGGCCTCAAAGATCCGACACCCGTGCTTGTCTTGCAGCCACGTGGC
CACGTGACACACACTGTTGGGATGGGAGAGGGTGATCTTGTGGTAGTCGCCGGCATGGTT
GCCGTAGCCCATAATGGAACGGCGCGTGACCTTCTCCACCGAGACCCGGCAGGGGGTCCT
GCGGTCGAAGGTGCTGGCCTTGAGGGCGCTGAGGACTGCAAACTCCACGTCCAGACCCTG
AGGCGCGCTGGCGTAGAAGTAGGCCTGCTGCCCAAACACGTTCACACACACGCTGGCCCC
ATCGGCCTTGCGCCGGCCCAGTAGCTTGATGACGATGCCACATGGCACCACATACCCCTG
TTTATCCGATGGAATGACGGCGCATTTCTCGTGCGTGTACACCGTCTCGAGTATGTCGTA
GACATGGAAGTCCAGAGGGCTTCCGTGGGTGTCTGCCTCCGGCCTTGCCGTGCCCTCTTG
GGCACGCTGGCGCCACCACATGCCCTTTCCATCCTCGTCACCCCCCACCACCGTCAGGGA
GTCTTGGTAGAAGCACAGGGGGGGCTGAGGCCCCCGCACATCCACCACCCCTGCGGCGCC
TGGTGTCTGGAAACACTTGGGAATGAGACGCAGGTACTCCTTGTCAGGCTTTTTCAGAAG
GCCTTTATTAGGTCTTAGGAAAGGGTTATAGAAGAGTCCCCCAGACAT
Target 4 GenBank Gene ID
Target 4 GeneCard ID Not Available
Target 4 GenAtlas ID Not Available
Target 4 HGNC ID Not Available
Target 4 Chromosome Location Not Available
Target 4 Locus Not Available
Target 4 SNPs Not Available
Target 4 General References
  1. Baer R, Bankier AT, Biggin MD, Deininger PL, Farrell PJ, Gibson TJ, Hatfull G, Hudson GS, Satchwell SC, Seguin C, et al.: DNA sequence and expression of the B95-8 Epstein-Barr virus genome. Nature. 1984 Jul 19-25;310(5974):207-11. [PubMed Link Image]
  2. Bankier AT, Deininger PL, Farrell PJ, Barrell BG: Sequence analysis of the 17,166 base-pair EcoRI fragment C of B95-8 Epstein-Barr virus. Mol Biol Med. 1983 Jul;1(1):21-45. [PubMed Link Image]
Target 4 Drug References
  1. Suzuki M, Okuda T, Shiraki K: Synergistic antiviral activity of acyclovir and vidarabine against herpes simplex virus types 1 and 2 and varicella-zoster virus. Antiviral Res. 2006 Nov;72(2):157-61. Epub 2006 May 30. [PubMed Link Image]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  3. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 5 [top]
Target 5 ID 4105
Target 5 Name Thymidine kinase
Target 5 Synonyms
  1. EC 2.7.1.21
Target 5 Gene Name 36
Target 5 Protein Sequence >Thymidine kinase 
MSTDKTDVKMGVLRIYLDGAYGIGKTTAAEEFLHHFAITPNRILLIGEPLSYWRNLAGED
AICGIYGTQTRRLNGDVSPEDAQRLTAHFQSLFCSPHAIMHAKISALMDTSTSDLVQVNK
EPYKIMLSDQHPIASTICFPLSRYLVGDMSPAALPGLLFTLPAEPPGTNLVVCTVSLPSH
LSRVSKRARPGETVNLPFVMVLRNVYIMLINTIIFLKTNNWHAGWNTLSFCNDVFKQKLQ
KSECIKLREVPGIEDTLFAVLKLPELCGEFGNILPLWAWGMETLSNCLRSMSPFVLSLEQ
TPQHAAQELKTLLPQMTPANMSSGAWNILKELVNAVQDNTS
Target 5 Number of Residues 346
Target 5 Molecular Weight 37815
Target 5 Theoretical pI 6.98
Target 5 GO Classification
Function
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
kinase activity
nucleobase, nucleoside, nucleotide kinase activity
nucleoside kinase activity
deoxynucleoside kinase activity
thymidine kinase activity
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
nucleotide metabolism
pyrimidine nucleotide metabolism
pyrimidine nucleotide biosynthesis
pyrimidine nucleoside monophosphate biosynthesis
pyrimidine ribonucleoside monophosphate biosynthesis
TMP biosynthesis
Component
Not Available
Target 5 General Function Not Available
Target 5 Specific Function ATP + thymidine = ADP + thymidine 5'- phosphate
Target 5 Pathways
Name SMPDB Link KEGG Link
Pyrimidine metabolism SMP00046 Link Image map00240 Link Image
Target 5 Reactions
  • ATP + thymidine = ADP + thymidine 5'-phosphate
Target 5 Pfam Domain Function
Target 5 Signals
  • None
Target 5 Transmembrane Regions
  • None
Target 5 Essentiality Essential
Target 5 GenBank ID Protein Not Available
Target 5 UniProtKB/Swiss-Prot ID P14342 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name KITH_VZV7 Link Image
Target 5 PDB ID 1OSN Link Image
Target 5 PDB File Show
Target 5 3D Structure
Target 5 Cellular Location Not Available
Target 5 Gene Sequence Not Available
Target 5 GenBank Gene ID
Target 5 GeneCard ID Not Available
Target 5 GenAtlas ID Not Available
Target 5 HGNC ID Not Available
Target 5 Chromosome Location Not Available
Target 5 Locus Not Available
Target 5 SNPs SNPJam Report Link Image
Target 5 General References
  1. Sawyer MH, Inchauspe G, Biron KK, Waters DJ, Straus SE, Ostrove JM: Molecular analysis of the pyrimidine deoxyribonucleoside kinase gene of wild-type and acyclovir-resistant strains of varicella-zoster virus. J Gen Virol. 1988 Oct;69 ( Pt 10):2585-93. [PubMed Link Image]
Target 5 Drug References
  1. Henrot A: [Mother-infant and indirect transmission of HSV infection: treatment and prevention] Ann Dermatol Venereol. 2002 Apr;129(4 Pt 2):533-49. [PubMed Link Image]
  2. Suzuki M, Okuda T, Shiraki K: Synergistic antiviral activity of acyclovir and vidarabine against herpes simplex virus types 1 and 2 and varicella-zoster virus. Antiviral Res. 2006 Nov;72(2):157-61. Epub 2006 May 30. [PubMed Link Image]
  3. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  4. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.