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Showing drug card for Aciclovir (DB00787)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:04:45
Primary Accession Number DB00787
Secondary Accession Number
  • APRD00567
  • EXPT00406
Name Aciclovir
Drug Type
  • Approved
  • Small Molecule
Description A guanosine analog that acts as an antimetabolite. Viruses are especially susceptible. Used especially against herpes. [PubChem]
Synonyms
  1. 9-Hyroxyethoxymethylguanine
  2. AC2
  3. Aciclovier
  4. Aciclovir Sodium
  5. Acycloguanosine
  6. Acyclovir
  7. Acyclovir Sodium
  8. Wellcome-248u
Brand Names
  1. Alti-Acyclovir
  2. Avirax
  3. Vipral
  4. Virorax
  5. Zovir
  6. Zovirax
Brand Mixtures
  1. Zovirax Injection (Zovirax sodium)
Chemical IUPAC Name 2-amino-9-(2-hydroxyethoxymethyl)-3H-purin-6-one
Chemical Formula C8H11N5O3
Chemical Structure Structure
CAS Registry Number 59277-89-3
InChI Identifier InChI=1/C8H11N5O3/c9-8-11-6-5(7(15)12-8)10-3-13(6)4-16-2-1-14/h3,14H,1-2,4H2,(H3,9,11,12,15)/f/h11H,9H2
InChI Key MKUXAQIIEYXACX-NTGMBSGFCM
KEGG Drug D00222 Link Image
KEGG Compound C06810 Link Image
PubChem Compound 2022 Link Image
PubChem Substance 7847289 Link Image
ChEBI ID Not Available
PharmGKB ID PA448045 Link Image
HET ID AC2 Link Image
GenBank ID Not Available
Drug ID Number [DIN] 02242784 Link Image
RxList Link http://www.rxlist.com/cgi/generic/acyclo.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Aciclovir Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS)
Synthesis Reference H. Matsumoto et al., Chem. Pharm. Bull. 35, 1153 (1988)
Average Molecular Weight 225.2046
Monoisotopic Molecular Weight 225.0862
State Solid
Melting Point 256.5 - 257 oC
Experimental Water Solubility 1.62 mg/mL at 22 oC [KRISTL,A et al. (1993)] Source: PhysProp
Predicted Water Solubility 9.08e+00 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity -1.56 [KRISTL,A ET AL. (1993)] Source: PhysProp
Predicted LogP -0.94 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -1.39 Calculated using ALOGPS
Experimental Caco2 Permeability -6.15 [ADME Research, USCD]
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 2KI5 Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES NC1=NC(=O)C2=C(N1)N(COCCO)C=N2
Canonical SMILES NC1=NC(=O)C2=C(N1)N(COCCO)C=N2
Drug Category
  • Antiviral Agents
  • Nucleosides and Nucleotides
ATC Codes
AHFS Codes
  • 08:18.32
  • 84:04.06
Indication For the treatment and management of herpes zoster (shingles), genital herpes, and chickenpox
Pharmacology Aciclovir (INN) or acyclovir (USAN, former BAN) is a synthetic deoxyguanosine analog and it is the prototype antiviral agent that is activated by viral thymidine kinase. The selective activity of aciclovir is due to its affinity for the thymidine kinase enzyme encoded by HSV and VZV.
Mechanism of Action Viral (HSV-1, HSV-2 and VZV) thymidine kinase converts aciclovir to the aciclovir monophosphate, which is then converted to the diphosphate by cellular guanylate kinase, and finally to the triphosphate by phosphoglycerate kinase, phosphoenolpyruvate carboxykinase, and pyruvate kinase. Aciclovir triphosphate competitively inhibits viral DNA polymerase and competes with the natural deoxyguanosine triphosphate, for incorporation into viral DNA. Once incorporated, aciclovir triphosphate inhibits DNA synthesis by acting as a chain terminator.
Absorption Oral: bioavailability 10 to 20%
Toxicity Aciclovir may cause nephrotoxicity (crystallization of aciclovir within renal tubules, elevation of serum creatinine, transient), and neurotoxicity (coma, hallucinations, lethargy, seizures, tremors). Nephrotoxicity and neurotoxicity usually resolve after cessation of aciclovir therapy. However, there is no well-defined relationship between aciclovir concentrations in the blood and these adverse effects.
Protein Binding 9%-33%
Biotransformation Hepatic, the only major urinary metabolite that has been detected is 9-carboxymethoxymethylguanine.
Half Life 2.5-3.3 hours
Dosage Forms
Form Route
Cream Topical
Ointment Topical
Powder, for solution Intravenous
Solution Intravenous
Suspension Oral
Tablet Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Aminophylline Acyclovir increases the effect and toxicity of theophylline
Dyphylline Acyclovir increases the effect and toxicity of theophylline
Dyphylline Increases the effect and toxicity of theophylline
Oxtriphylline Increases the effect and toxicity of theophylline
Theophylline Acyclovir increases the effect and toxicity of theophylline
Theophylline Increases the effect and toxicity of theophylline
Food Interactions
  • Increase liquid intake.
  • Take without regard to meals.
Pathways Not Available
General References
  1. O'Brien JJ, Campoli-Richards DM: Acyclovir. An updated review of its antiviral activity, pharmacokinetic properties and therapeutic efficacy. Drugs. 1989 Mar;37(3):233-309. [PubMed Link Image]
  2. Drugs.com Link Image
  3. Wikipedia Link Image
  4. RxList Link Image
Organisms Affected
  • Human Herpes Virus
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 1A2 (CYP1A2)
Targets
  1. Purine nucleoside phosphorylase
  2. DNA polymerase
  3. DNA polymerase
  4. Thymidine kinase
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 1A2 (CYP1A2)
Enzyme 1 Gene Name CYP1A2
Enzyme 1 SwissProt ID P05177 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >P05177|CP1A2_HUMAN Cytochrome P450 1A2 - Homo sapiens (Human). 
MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKN
PHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDG
QSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELM
AGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFP
ILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGN
LIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLS
DRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPEL
WEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLE
FSVPPGVKVDLTPIYGLTMKHARCEHVQARRFSIN
Drug Target 1 [top]
Target 1 ID 277
Target 1 Name Purine nucleoside phosphorylase
Target 1 Synonyms
  1. EC 2.4.2.1
  2. Inosine phosphorylase
  3. PNP
Target 1 Gene Name NP
Target 1 Protein Sequence >Purine nucleoside phosphorylase 
MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRST
VPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGL
NPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQ
MGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSL
ITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
Target 1 Number of Residues 293
Target 1 Molecular Weight 32118
Target 1 Theoretical pI 6.95
Target 1 GO Classification
Function
purine-nucleoside phosphorylase activity
catalytic activity
transferase activity
transferase activity, transferring glycosyl groups
transferase activity, transferring pentosyl groups
Process
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
Component
Not Available
Target 1 General Function Nucleotide transport and metabolism
Target 1 Specific Function Not Available
Target 1 Pathways
Name SMPDB Link KEGG Link
Nicotinate and nicotinamide metabolism SMP00048 Link Image map00760 Link Image
Purine metabolism SMP00050 Link Image map00230 Link Image
Pyrimidine metabolism SMP00046 Link Image map00240 Link Image
Target 1 Reactions
  • purine nucleoside + phosphate = purine + alpha-D-ribose 1-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 35565 Link Image
Target 1 UniProtKB/Swiss-Prot ID P00491 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name PNPH_HUMAN Link Image
Target 1 PDB ID 1RT9 Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location Not Available
Target 1 Gene Sequence >870 bp 
ATGGAGAACGGATACACCTATGAAGATTATAAGAACACTGCAGAATGGCTTCTGTCTCAT
ACTAAGCACCGACCTCAAGTTGCAATAATCTGTGGTTCTGGATTAGGAGGTCTGACTGAT
AAATTAACTCAGGCCCAGATCTTTGACTACAGTGAAATCCCCAACTTTCCTCGAAGTACA
GTGCCAGGTCATGCTGGCCGACTGGTGTTTGGGTTCCTGAATGGCAGGGCCTGTGTGATG
ATGCAGGGCAGGTTCCACATGTATGAAGGGTACCCACTCTGGAAGGTGACATTCCCAGTG
AGGGTTTTCCACCTTCTGGGTGTGGACACCCTGGTAGTCACCAATGCAGCAGGAGGGCTG
AACCCCAAGTTTGAGGTTGGAGATATCATGCTGATCCGTGACCATATCAACCTACCTGGT
TTCAGTGGTCAGAACCCTCTCAGAGGGCCCAATGATGAAAGGTTTGGAGATCGTTTCCCT
GCCATGTCTGATGCCTACGACCGGACTATGAGGCAGAGGGCTCTCAGTACCTGGAAACAA
ATGGGGGAGCAACGTGAGCTACAGGAAGGCACCTATGTGATGGTGGCAGGCCCCAGCTTT
GAGACTGTGGCAGAATGTCGTGTGCTGCAGAAGCTGGGAGCAGACGCTGTTGGCATGAGT
ACAGTACCAGAAGTTATCGTTGCACGGCACTGTGGACTTCGAGTCTTTGGCTTCTCACTC
ATCACTAACAAGGTCATCATGGATTATGAAAGCCTGGAGAAGGCCAACCATGAAGAAGTC
TTAGCAGCTGGCAAACAAGCTGCACAGAAATTGGAACAGTTTGTCTCCATTCTTATGGCC
AGCATTCCACTCCCTGACAAAGCCAGTTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID NP Link Image
Target 1 GenAtlas ID NP Link Image
Target 1 HGNC ID HGNC:7892 Link Image
Target 1 Chromosome Location 14
Target 1 Locus 14q13.1
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Yu L, Kalla K, Guthrie E, Vidrine A, Klimecki WT: Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans. Environ Health Perspect. 2003 Aug;111(11):1421-7. [PubMed Link Image]
  2. Aust MR, Andrews LG, Barrett MJ, Norby-Slycord CJ, Markert ML: Molecular analysis of mutations in a patient with purine nucleoside phosphorylase deficiency. Am J Hum Genet. 1992 Oct;51(4):763-72. [PubMed Link Image]
  3. Ealick SE, Rule SA, Carter DC, Greenhough TJ, Babu YS, Cook WJ, Habash J, Helliwell JR, Stoeckler JD, Parks RE Jr, et al.: Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution. J Biol Chem. 1990 Jan 25;265(3):1812-20. [PubMed Link Image]
  4. Williams SR, Gekeler V, McIvor RS, Martin DW Jr: A human purine nucleoside phosphorylase deficiency caused by a single base change. J Biol Chem. 1987 Feb 15;262(5):2332-8. [PubMed Link Image]
  5. Williams SR, Goddard JM, Martin DW Jr: Human purine nucleoside phosphorylase cDNA sequence and genomic clone characterization. Nucleic Acids Res. 1984 Jul 25;12(14):5779-87. [PubMed Link Image]
  6. Pannicke U, Tuchschmid P, Friedrich W, Bartram CR, Schwarz K: Two novel missense and frameshift mutations in exons 5 and 6 of the purine nucleoside phosphorylase (PNP) gene in a severe combined immunodeficiency (SCID) patient. Hum Genet. 1996 Dec;98(6):706-9. [PubMed Link Image]
Target 1 Drug References Not Available
Drug Target 2 [top]
Target 2 ID 338
Target 2 Name DNA polymerase
Target 2 Synonyms
  1. EC 2.7.7.7
Target 2 Gene Name UL30
Target 2 Protein Sequence >DNA polymerase 
MFSGGGGPLSPGGKSAARAASGFFAPAGPRGASRGPPPCLRQNFYNPYLAPVGTQQKPTG
PTQRHTYYSECDEFRFIAPRVLDEDAPPEKRAGVHDGHLKRAPKVYCGGDERDVLRVGSG
GFWPRRSRLWGGVDHAPAGFNPTVTVFHVYDILENVEHAYGMRAAQFHARFMDAITPTGT
VITLLGLTPEGHRVAVHVYGTRQYFYMNKEEVDRHLQCRAPRDLCERMAAALRESPGASF
RGISADHFEAEVVERTDVYYYETRPALFYRVYVRSGRVLSYLCDNFCPAIKKYEGGVDAT
TRFILDNPGFVTFGWYRLKPGRNNTLAQPAAPMAFGTSSDVEFNCTADNLAIEGGMSDLP
AYKLMCFDIECKAGGEDELAFPVAGHPEDLVIQISCLLYDLSTTALEHVLLFSLGSCDLP
ESHLNELAARGLPTPVVLEFDSEFEMLLAFMTLVKQYGPEFVTGYNIINFDWPFLLAKLT
DIYKVPLDGYGRMNGRGVFRVWDIGQSHFQKRSKIKVNGMVNIDMYGIITDKIKLSSYKL
NAVAEAVLKDKKKDLSYRDIPAYYAAGPAQRGVIGEYCIQDSLLVGQLFFKFLPHLELSA
VARLAGINITRTIYDGQQIRVFTCLLRLADQKGFILPDTQGRFRGAGGEAPKRPAAARED
EERPEEEGEDEDEREEGGGEREPEGARETAGRHVGYQGARVLDPTSGFHVNPVVVFDFAS
LYPSIIQAHNLCFSTLSLRADAVAHLEAGKDYLEIEVGGRRLFFVKAHVRESLLSILLRD
WLAMRKQIRSRIPQSSPEEAVLLDKQQAAIKVVCNSVYGFTGVQHGLLPCLHVAATVTTI
GREMLLATREYVHARWAAFEQLLADFPEAADMRAPGPYSMRIIYGDTDSIFVLCRGLTAA
GLTAVGDKMASHISRALFLPPIKLECEKTFTKLLLIAKKKYIGVIYGGKMLIKGVDLVRK
NNCAFINRTSRALVDLLFYDDTVSGAAAALAERPAEEWLARPLPEGLQAFGAVLVDAHRR
ITDPERDIQDFVLTAELSRHPRAYTNKRLAHLTVYYKLMARRAQVPSIKDRIPYVIVAQT
REVEETVARLAALRELDAAAPGDEPAPPAALPSPAKRPRETPSPADPPGGASKPRKLLVS
ELAEDPAYAIAHGVALNTDYYFSHLLGAACVTFKALFGNNAKITESLLKRFIPEVWHPPD
DVAARLRTAGFGAVGAGATAEETRRMLHRAFDTLA
Target 2 Number of Residues 1255
Target 2 Molecular Weight 136422
Target 2 Theoretical pI 7.31
Target 2 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 2 General Function Replication, recombination and repair
Target 2 Specific Function Not Available
Target 2 Pathways
Name SMPDB Link KEGG Link
DNA polymerase map03030 Link Image
Purine metabolism SMP00050 Link Image map00230 Link Image
Pyrimidine metabolism SMP00046 Link Image map00240 Link Image
Target 2 Reactions
  • deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 59530 Link Image
Target 2 UniProtKB/Swiss-Prot ID P04293 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name DPOL_HHV11 Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Nucleus
Target 2 Gene Sequence >3708 bp 
ATGTTTTCCGGTGGCGGCGGCCCGCTGTCCCCCGGAGGAAAGTCGGCGGCCAGGGCGGCG
TCCGGGTTTTTTGCGCCCGCCGGCCCTCGCGGAGCCAGCCGGGGACCCCCGCCTTGTTTG
AGGCAAAACTTTTACAACCCCTACCTCGCCCCAGTCGGGACGCAACAGAAGCCGACCGGG
CCAACCCAGCGCCATACGTACTATAGCGAATGCGATGAATTTCGATTCATCGCCCCGCGG
GTGCTGGACGAGGATGCCCCCCCGGAGAAGCGCGCCGGGGTGCACGACGGTCACCTCAAG
CGCGCCCCCAAGGTGTACTGCGGGGGGGACGAGCGCGACGTCCTCCGCGTCGGGTCGGGC
GGCTTCTGGCCGCGGCGCTCGCGCCTGTGGGGCGGCGTGGACCACGCCCCGGCGGGGTTC
AACCCCACCGTCACCGTCTTTCACGTGTACGACATCCTGGAGAACGTGGAGCACGCGTAC
GGCATGCGCGCGGCCCAGTTCCACGCGCGGTTTATGGACGCCATCACACCGACGGGGACC
GTCATCACGCTCCTGGGCCTGACTCCGGAAGGCCACCGGGTGGCCGTTCACGTTTACGGC
ACGCGGCAGTACTTTTACATGAACAAGGAGGAGGTCGACAGGCACCTACAATGCCGCGCC
CCACGAGATCTCTGCGAGCGCATGGCCGCGGCCCTGCGCGAGTCCCCGGGCGCGTCGTTC
CGCGGCATCTCCGCGGACCACTTCGAGGCGGAGGTGGTGGAGCGCACCGACGTGTACTAC
TACGAGACGCGCCCCGCTCTGTTTTACCGCGTCTACGTCCGAAGCGGGCGTGTGCTGTCG
TACCTGTGCGACAACTTCTGCCCGGCCATCAAGAAGTACGAGGGTGGGGTCGACGCCACC
ACCCGGTTCATCCTGGACAACCCCGGGTTCGTCACCTTCGGCTGGTACCGTCTCAAACCG
GGCCGGAACAACACGCTAGCCCAGCCGGCGGCCCCGATGGCCTTCGGGACATCCAGCGAC
GTCGAGTTTAACTGTACGGCGGACAACCTGGCCATCGAGGGGGGCATGAGCGACCTACCG
GCATACAAGCTCATGTGCTTCGATATCGAATGCAAGGCGGGGGGGGAGGACGAGCTGGCC
TTTCCGGTGGCCGGGCACCCGGAGGACCTGGTCATCCAGATATCCTGTCTGCTCTACGAC
CTGTCCACCACCGCCCTGGAGCACGTCCTCCTGTTTTCGCTCGGTTCCTGCGACCTCCCC
GAATCCCACCTGAACGAGCTGGCGGCCAGGGGCCTGCCCACGCCCGTGGTTCTGGAATTC
GACAGCGAATTCGAGATGCTGTTGGCCTTCATGACCCTTGTGAAACAGTACGGCCCCGAG
TTCGTGACCGGGTACAACATCATCAACTTCGACTGGCCCTTCTTGCTGGCCAAGCTGACG
GACATTTACAAGGTCCCCCTGGACGGGTACGGCCGCATGAACGGCCGGGGCGTGTTTCGC
GTGTGGGACATAGGCCAGAGCCACTTCCAGAAGCGCAGCAAGATAAAGGTGAACGGCATG
GTGAACATCGACATGTACGGGATTATAACCGACAAGATCAAGCTCTCGAGCTACAAGCTC
AACGCCGTGGCCGAAGCCGTCCTGAAGGACAAGAAGAAGGACCTGAGCTATCGCGACATC
CCCGCCTACTACGCCGCCGGGCCCGCGCAACGCGGGGTGATCGGCGAGTACTGCATACAG
GATTCCCTGCTGGTGGGCCAGCTGTTTTTTAAGTTTTTGCCCCATCTGGAGCTCTCGGCC
GTCGCGCGCTTGGCGGGTATTAACATCACCCGCACCATCTACGACGGCCAGCAGATCCGC
GTCTTTACGTGCCTGCTGCGCCTGGCCGACCAGAAGGGCTTTATTCTGCCGGACACCCAG
GGGCGATTTAGGGGCGCCGGGGGGGAGGCGCCCAAGCGTCCGGCCGCAGCCCGGGAGGAC
GAGGAGCGGCCAGAGGAGGAGGGGGAGGACGAGGACGAACGCGAGGAGGGCGGGGGCGAG
CGGGAGCCGGAGGGCGCGCGGGAGACCGCCGGCAGGCACGTGGGGTACCAGGGGGCCAGG
GTCCTTGACCCCACTTCCGGGTTTCACGTGAACCCCGTGGTGGTGTTCGACTTTGCCAGC
CTGTACCCCAGCATCATCCAGGCCCACAACCTGTGCTTCAGCACGCTCTCCCTGAGGGCC
GACGCAGTGGCGCACCTGGAGGCGGGCAAGGACTACCTGGAGATCGAGGTGGGGGGGCGA
CGGCTGTTCTTCGTCAAGGCTCACGTGCGAGAGAGCCTCCTCAGCATCCTCCTGCGGGAC
TGGCTCGCCATGCGAAAGCAGATCCGCTCGCGGATTCCCCAGAGCAGCCCCGAGGAGGCC
GTGCTCCTGGACAAGCAGCAGGCCGCCATCAAGGTCGTGTGTAACTCGGTGTACGGGTTC
ACGGGAGTGCAGCACGGACTCCTGCCGTGCCTGCACGTTGCCGCGACGGTGACGACCATC
GGCCGCGAGATGCTGCTCGCGACCCGCGAGTACGTCCACGCGCGCTGGGCGGCCTTCGAA
CAGCTCCTGGCCGATTTCCCGGAGGCGGCCGACATGCGCGCCCCCGGGCCCTATTCCATG
CGCATCATCTACGGGGACACGGACTCCATCTTTGTGCTGTGCCGCGGCCTCACGGCCGCC
GGGCTGACGGCCGTGGGCGACAAGATGGCGAGCCACATCTCGCGCGCGCTGTTTCTGCCC
CCCATCAAACTCGAGTGCGAAAAGACGTTCACCAAGCTGCTGCTGATCGCCAAGAAAAAG
TACATCGGCGTCATCTACGGGGGTAAGATGCTCATCAAGGGCGTGGATCTGGTGCGCAAA
AACAACTGCGCGTTTATCAACCGCACCTCCAGGGCCCTGGTCGACCTGCTGTTTTACGAC
GATACCGTCTCCGGAGCGGCCGCCGCGTTAGCCGAGCGCCCCGCGGAGGAGTGGCTGGCG
CGACCCCTGCCCGAGGGACTGCAGGCGTTCGGGGCCGTCCTCGTAGACGCCCATCGGCGC
ATCACCGACCCGGAGAGGGACATCCAGGACTTTGTCCTCACCGCCGAACTGAGCAGACAC
CCGCGCGCGTACACCAACAAGCGCCTGGCCCACCTGACGGTGTATTACAAGCTCATGGCC
CGCCGCGCGCAGGTCCCGTCCATCAAGGACCGGATCCCGTACGTGATCGTGGCCCAGACC
CGCGAGGTAGAGGAGACGGTCGCGCGGCTGGCCGCCCTCCGCGAGCTAGACGCCGCCGCC
CCAGGGGACGAGCCCGCCCCCCCCGCGGCCCTGCCCTCCCCGGCCAAGCGCCCCCGGGAG
ACGCCGTCGCCTGCCGACCCCCCGGGAGGCGCGTCCAAGCCCCGCAAGCTGCTGGTGTCC
GAGCTGGCCGAGGATCCCGCATACGCCATTGCCCACGGCGTCGCCCTGAACACGGACTAT
TACTTCTCCCACCTGTTGGGGGCGGCGTGCGTGACATTCAAGGCCCTGTTTGGGAATAAC
GCCAAGATCACCGAGAGTCTGTTAAAAAGGTTTATTCCCGAAGTGTGGCACCCCCCGGAC
GACGTGGCCGCGCGGCTCCGGACCGCAGGGTTCGGGGCGGTGGGTGCCGGCGCTACGGCG
GAGGAAACTCGTCGAATGTTGCATAGAGCCTTTGATACTCTAGCATGA
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 Not Available
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. McGeoch DJ, Dalrymple MA, Davison AJ, Dolan A, Frame MC, McNab D, Perry LJ, Scott JE, Taylor P: The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1. J Gen Virol. 1988 Jul;69 ( Pt 7):1531-74. [PubMed Link Image]
  2. Quinn JP, McGeoch DJ: DNA sequence of the region in the genome of herpes simplex virus type 1 containing the genes for DNA polymerase and the major DNA binding protein. Nucleic Acids Res. 1985 Nov 25;13(22):8143-63. [PubMed Link Image]
Target 2 Drug References
  1. Liu S, Knafels JD, Chang JS, Waszak GA, Baldwin ET, Deibel MR Jr, Thomsen DR, Homa FL, Wells PA, Tory MC, Poorman RA, Gao H, Qiu X, Seddon AP: Crystal structure of the herpes simplex virus 1 DNA polymerase. J Biol Chem. 2006 Jun 30;281(26):18193-200. Epub 2006 Apr 24. [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]
  5. Sergerie Y, Boivin G: Hydroxyurea enhances the activity of acyclovir and cidofovir against herpes simplex virus type 1 resistant strains harboring mutations in the thymidine kinase and/or the DNA polymerase genes. Antiviral Res. 2007 Sep 17;. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 697
Target 3 Name DNA polymerase
Target 3 Synonyms
  1. EC 2.7.7.7
Target 3 Gene Name 28
Target 3 Protein Sequence >DNA polymerase 
MAIRTGFCNPFLTQASGIKYNPRTGRGSNREFLHSYKTTMSSFQFLAPKCLDEDVPMEER
KGVHVGTLSRPPKVYCNGKEVPILDFRCSSPWPRRVNIWGEIDFRGDKFDPRFNTFHVYD
IVETTEAASNGDVSRFATATRPLGTVITLLGMSRCGKRVAVHVYGICQYFYINKAEVDTA
CGIRSGSELSVLLAECLRSSMITQNDATLNGDKNAFHGTSFKSASPESFRVEVIERTDVY
YYDTQPCAFYRVYSPSSKFTNYLCDNFHPELKKYEGRVDATTRFLMDNPGFVSFGWYQLK
PGVDGERVRVRPASRQLTLSDVEIDCMSDNLQAIPNDDSWPDYKLLCFDIECKSGGSNEL
AFPDATHLEDLVIQISCLLYSIPRQSLEHILLFSLGSCDLPQRYVQEMKDAGLPEPTVLE
FDSEFELLIAFMTLVKQYAPEFATGYNIVNFDWAFIMEKLNSIYSLKLDGYGSINRGGLF
KIWDVGKSGFQRRSKVKINGLISLDMYAIATEKLKLSSYKLDSVAREALNESKRDLPYKD
IPGYYASGPNTRGIIGEYCIQDSALVGKLFFKYLPHLELSAVARLARITLTKAIYDGQQV
RIYTCLLGLASSRGFILPDGGYPATFEYKDVIPDVGDVEEEMDEDESVSPTGTSSGRNVG
YKGARVFDPDTGFYIDPVVVLDFASLYPSIIQAHNLCFTTLTLNFETVKRLNPSDYATFT
VGGKRLFFVRSNVRESLLGVLLKDWLAMRKAIRARIPGSSSDEAVLLDKQQAAIKVVCNS
VYGFTGVAQGFLPCLYVAATVTTIGRQMLLSTRDYIHNNWAAFERFITAFPDIESSVLSQ
KAYEVKVIYGDTDSVFIRFKGVSVEGIAKIGEKMAHIISTALFCPPIKLECEKTFIKLLL
ITKKKYIGVIYGGKVLMKGVDLVRKNNCQFINDYARKLVELLLYDDTVSRAAAEASCVSI
AEWNRRAMPSGMAGFGRIIADAHRQITSPKLDINKFVMTAELSRPPSAYINRRLAHLTVY
YKLVMRQGQIPNVRERIPYVIVAPTDEVEADAKSVALLRGDPLQNTAGKRCGEAKRKLII
SDLAEDPIHVTSHGLSLNIDYYFSHLIGTASVTFKALFGNDTKLTERLLKRFIPETRVVN
VKMLNRLQAAGFVCIHAPCWDNKMNTEAEITEEEQSHQIMRRVFCIPKAILHQS
Target 3 Number of Residues 1213
Target 3 Molecular Weight 134049
Target 3 Theoretical pI 7.94
Target 3 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 3 General Function Replication, recombination and repair
Target 3 Specific Function Not Available
Target 3 Pathways
Name SMPDB Link KEGG Link
DNA polymerase map03030 Link Image
Purine metabolism SMP00050 Link Image map00230 Link Image
Pyrimidine metabolism SMP00046 Link Image map00240 Link Image
Target 3 Reactions
  • deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Essential
Target 3 GenBank ID Protein 60016 Link Image
Target 3 UniProtKB/Swiss-Prot ID P09252 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name DPOL_VZVD Link Image
Target 3 PDB ID Not Available
Target 3 Cellular Location
  • Nucleus
Target 3 Gene Sequence >3585 bp 
TTAACTTTGATGGAGAATTGCTTTTGGAATACAAAAGACTCTACGCATTATTTGATGACT
TTGTTCCTCCTCGGTGATTTCAGCTTCAGTGTTCATTTTATTATCCCAGCACGGGGCGTG
TATACAAACAAAGCCTGCCGCCTGCAAGCGGTTTAGCATTTTAACGTTAACAACTCGTGT
CTCTGGAATAAAACGTTTTAAAAGCCGTTCTGTGAGTTTAGTGTCGTTTCCAAATAACGC
CTTAAAAGTTACACTCGCCGTCCCAATGAGATGAGAAAAATAATAGTCAATGTTTAAAGA
CAGCCCGTGTGATGTTACGTGAATGGGATCTTCCGCTAAGTCAGATATTATTAACTTACG
CTTTGCTTCCCCACACCGTTTACCTGCGGTATTCTGTAAAGGATCTCCACGTAGCAAAGC
TACACTTTTTGCATCAGCCTCCACTTCGTCTGTGGGGGCCACAATAACATAAGGGATGCG
TTCTCGAACGTTTGGGATTTGACCCTGTCTCATTACTAATTTATAATATACTGTTAAGTG
AGCCAAGCGACGGTTTATGTAGGCGGATGGTGGACGACTAAGCTCGGCCGTCATAACAAA
CTTATTAATATCCAATTTGGGTGATGTAATCTGGCGATGTGCATCTGCAATTATGCGTCC
AAACCCGGCCATCCCAGACGGCATGGCCCGTCTATTCCATTCAGCAATGGAAACACACGA
CGCCTCCGCCGCAGCACGCGAGACGGTGTCGTCATATAACAACAGTTCTACAAGTTTGCG
GGCATAATCGTTAATAAATTGACAGTTGTTTTTTCTAACCAAGTCGACTCCCTTCATTAA
AACCTTTCCGCCGTAAATTACCCCAATGTACTTTTTCTTTGTTATAAGCAAAAGTTTTAT
AAAAGTTTTTTCACACTCCAACTTTATAGGAGGACAAAACAGAGCCGTTGAAATTATATG
TGCCATTTTCTCGCCGATTTTAGCTATCCCCTCAACACTAACACCCTTGAATCGGATAAA
CACAGAATCCGTATCTCCATATATAACCTTTACCTCGTACGCTTTTTGGGAGAGAACGCT
ACTTTCAATGTCTGGAAACGCTGTAATAAAACGTTCAAATGCGGCCCAGTTATTATGAAT
ATAATCTCTGGTACTTAATAACATTTGACGGCCAATTGTAGTGACAGTGGCCGCTACGTA
TAAACATGGCAGAAATCCCTGCGCAACTCCAGTAAAACCGTACACGGAATTACAAACTAC
TTTTATCGCGGCTTGTTGTTTGTCTAATAACACTGCTTCATCTGAAGAACTTCCGGGTAT
GCGCGCTCTAATAGCCTTGCGCATAGCCAACCAGTCTTTTAAAAGAACACCCAGCAGACT
TTCTCGAACGTTAGAGCGCACAAAAAAAAGACGTTTTCCTCCAACTGTAAAGGTGGCATA
ATCGGATGGATTCAAACGTTTAACCGTCTCAAAATTTAACGTTAGCGTGGTAAAACATAA
GTTATGGGCCTGAATTATACTTGGATATAAACTTGCAAAATCCAATACGACCACCGGATC
GATATAAAATCCCGTATCAGGGTCAAAAACCCTGGCTCCTTTATATCCTACATTTCGCCC
ACTTGACGTACCAGTGGGAGAAACGCTCTCGTCTTCATCCATCTCTTCCTCAACATCCCC
GACATCGGGAATAACATCCTTATATTCAAAAGTAGCTGGGTATCCCCCATCGGGTAAAAT
AAATCCTCGAGACGAAGCCAGTCCTAATAAACAGGTGTAAATCCTAACCTGCTGTCCGTC
GTAAATAGCCTTGGTTAAAGTAATTCTAGCTAGCCTTGCAACCGCGGATAACTCAAGGTG
TGGTAAATATTTAAAAAACAGTTTCCCCACAAGAGCCGAGTCTTGTATACAATATTCACC
AATAATTCCTCGTGTATTCGGTCCACTAGCGTAATATCCCGGAATGTCTTTGTAGGGCAA
ATCTCTCTTGGACTCATTTAGAGCTTCACGTGCAACCGAATCTAATTTATAACTCGAGAG
TTTTAATTTTTCAGTTGCAATTGCATACATATCCAGAGATATGAGACCGTTGATCTTTAC
CTTGCTTCGTCGCTGAAATCCGGATTTGCCAACATCCCATATCTTAAACAGACCCCCACG
GTTTATACTGCCATAACCATCAAGCTTGAGACTGTATATAGAATTAAGTTTCTCCATAAT
AAACGCCCAATCAAAATTAACAATGTTATAACCTGTGGCAAACTCGGGAGCGTACTGTTT
TACGAGGGTCATAAATGCAATTAATAGCTCGAATTCACTATCAAACTCCAGCACAGTCGG
CTCCGGTAACCCCGCGTCCTTCATTTCTTGTACATACCTTTGTGGTAAGTCACAAGAGCC
AAGGGAAAACAGTAAAATGTGTTCTAAAGACTGTCGAGGGATTGAATATAATAGACAAGA
AATTTGGATTACAAGATCCTCCAGATGTGTTGCATCGGGAAACGCCAGCTCATTAGATCC
TCCTGATTTACATTCAATATCGAAACATAACAACTTGTAGTCAGGCCATGAGTCATCGTT
TGGTATAGCCTGCAGATTATCCGACATGCAGTCAATTTCAACGTCGCTTAACGTTAATTG
GCGACTTGCCGGTCGAACTCGAACACGTTCCCCATCAACTCCAGGTTTTAGTTGATACCA
ACCAAAACTAACAAAGCCGGGATTATCCATTAGAAAACGAGTGGTAGCGTCTACCCGACC
TTCATACTTTTTCAACTCCGGGTGAAAGTTATCACAAAGATAATTTGTAAATTTAGATGA
GGGAGAATACACCCTGTAAAACGCACATGGCTGTGTATCGTAGTAATAAACATCTGTGCG
CTCAATAACCTCAACGCGAAAGCTTTCTGGAGATGCGCTTTTAAACGAGGTACCATGAAA
AGCGTTCTTGTCTCCATTTAACGTTGCATCATTTTGTGTTATCATAGAACTGCGTAAACA
CTCGGCAAGTAATACAGATAACTCGCTACCGGAACGTATGCCACAAGCGGTATCCACCTC
GGCTTTGTTTATATAAAAATATTGACAGATGCCGTATACATGAACTGCCACCCTTTTTCC
ACATCGGGACATGCCAAGTAAAGTAATAACGGTACCAAGCGGTCGTGTTGCAGTTGCAAA
CCGGGATACATCTCCATTAGACGCGGCTTCTGTTGTTTCGACAATATCATATACATGGAA
TGTGTTAAAGCGGGGGTCAAACTTATCCCCACGAAAGTCGATTTCCCCCCAAATATTCAC
GCGTCTAGGCCAGGGGCTGGAACAACGAAAATCCAGAATCGGAACTTCTTTTCCATTACA
GTAAACTTTAGGCGGTCGACTAAGTGTACCGACGTGAACCCCCTTTCGTTCTTCCATGGG
CACATCTTCATCTAAACATTTAGGGGCCAAAAATTGAAACGATGACATGGTAGTTTTGTA
ACTATGAAGAAATTCTCTGTTACTACCGCGCCCGGTTCTTGGGTTATATTTAATCCCTGA
TGCTTGGGTTAAAAAGGGATTACAAAACCCCGTTCTGATCGCCAT
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. Davison AJ, Scott JE: The complete DNA sequence of varicella-zoster virus. J Gen Virol. 1986 Sep;67 ( Pt 9):1759-816. [PubMed Link Image]
Target 3 Drug References
  1. Liu S, Knafels JD, Chang JS, Waszak GA, Baldwin ET, Deibel MR Jr, Thomsen DR, Homa FL, Wells PA, Tory MC, Poorman RA, Gao H, Qiu X, Seddon AP: Crystal structure of the herpes simplex virus 1 DNA polymerase. J Biol Chem. 2006 Jun 30;281(26):18193-200. Epub 2006 Apr 24. [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]
  5. Sergerie Y, Boivin G: Hydroxyurea enhances the activity of acyclovir and cidofovir against herpes simplex virus type 1 resistant strains harboring mutations in the thymidine kinase and/or the DNA polymerase genes. Antiviral Res. 2007 Sep 17;. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 2559
Target 4 Name Thymidine kinase
Target 4 Synonyms
  1. EC 2.7.1.21
Target 4 Gene Name TK
Target 4 Protein Sequence >Thymidine kinase 
MASYPCHQHASAFDQAARSRGHNNRRTALRPRRQQEATEVRPEQKMPTLLRVYIDGPHGM
GKTTTTQLLVALGSRDDIVYVPEPMTYWRVLGASETIANIYTTQHRLDQGEISAGDAAVV
MTSAQITMGMPYAVTDAVLAPHIGGEAGSSHAPPPALTLIFDRHPIAALLCYPAARYLMG
SMTPQAVLAFVALIPPTLPGTNIVLGALPEDRHIDRLAKRQRPGERLDLAMLAAIRRVYG
LLANTVRYLQCGGSWREDWGQLSGTAVPPQGAEPQSNAGPRPHIGDTLFTLFRAPELLAP
NGDLYNVFAWALDVLAKRLRSMHVFILDYDQSPAGCRDALLQLTSGMVQTHVTTPGSIPT
ICDLARTFAREMGEAN
Target 4 Number of Residues 382
Target 4 Molecular Weight 40973
Target 4 Theoretical pI 7.96
Target 4 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 4 General Function Involved in thymidine kinase activity
Target 4 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 4 Pathways
Name SMPDB Link KEGG Link
Pyrimidine metabolism SMP00046 Link Image map00240 Link Image
Target 4 Reactions
  • ATP + thymidine = ADP + thymidine 5'-phosphate
Target 4 Pfam Domain Function
Target 4 Signals
  • None
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 59524 Link Image
Target 4 UniProtKB/Swiss-Prot ID P03176 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name KITH_HHV11 Link Image
Target 4 PDB ID 1OF1 Link Image
Target 4 PDB File Show
Target 4 3D Structure
Target 4 Cellular Location Not Available
Target 4 Gene Sequence >1131 bp 
TCAGTTAGCCTCCCCCATCTCCCGGGCAAACGTGCGCGCCAGGTCGCAGATCGTCGGTAT
GGAGCCTGGGGTGGTGACGTGGGTCTGGACCATCCCGGAGGTAAGTTGCAGCAGGGCGTC
CCGGCAGCCGGCGGGCGATTGGTCGTAATCCAGGATAAAGACATGCATGGGACGGAGGCG
TTTGGCCAAGACGTCCAAAGCCCAGGCAAACACGTTATACAGGTCGCCGTTGGGGGCCAG
CAACTCGGGGGCCCGAAACAGGGTAAATAACGTGTCCCCGATATGGGGTCGTGGGCCCGC
GTTGCTCTGGGGCTCGGCACCCTGGGGCGGCACGGCCGCCCCCGAAAGCTGTCCCCAATC
CTCCCGCCACGACCCGCCGCCCTGCAGATACCGCACCGTATTGGCAAGCAGCCCATAAAC
GCGGCGAATCGCGGCCAGCATAGCCAGGTCAAGCCGCTCGCCGGGGCGCTGGCGTTTGGC
CAGGCGGTCGATGTGTCTGTCCTCCGGAAGGGCCCCCAACACGATGTTTGTGCCGGGCAA
GGTCGGCGGGATGAGGGCCACGAACGCCAGCACGGCCTGGGGGGTCATGCTGCCCATAAG
GTATCGCGCGGCCGGGTAGCACAGGAGGGCGGCGATGGGATGGCGGTCGAAGATGAGGGT
GAGGGCCGGGGGCGGGGCATGTGAGCTCCCAGCCTCCCCCCCGATATGAGGAGCCAGAAC
GGCGTCGGTCACGGCATAAGGCATGCCCATTGTTATCTGGGCGCTTGTCATTACCACCGC
CGCGTCCCCGGCCGATATCTCACCCTGGTCGAGGCGGTGTTGTGTGGTGTAGATGTTCGC
GATTGTCTCGGAAGCCCCCAACACCCGCCAGTAAGTCATCGGCTCGGGTACGTAGACGAT
ATCGTCGCGCGAACCCAGGGCCACCAGCAGTTGCGTGGTGGTGGTTTTCCCCATCCCGTG
GGGACCGTCTATATAAACCCGCAGTAGCGTGGGCATTTTCTGCTCCAGGCGGACTTCCGT
GGCTTTTTGTTGCCGGCGAGGGCGCAACGCCGTACGTCGGTTGTTATGGCCGCGAGAACG
CGCAGCCTGGTCGAACGCAGACGCGTGTTGATGGCAGGGGTACGAAGCCAT
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 MT
Target 4 Locus -
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. McGeoch DJ, Dalrymple MA, Davison AJ, Dolan A, Frame MC, McNab D, Perry LJ, Scott JE, Taylor P: The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1. J Gen Virol. 1988 Jul;69 ( Pt 7):1531-74. [PubMed Link Image]
  2. McKnight SL: The nucleotide sequence and transcript map of the herpes simplex virus thymidine kinase gene. Nucleic Acids Res. 1980 Dec 20;8(24):5949-64. [PubMed Link Image]
  3. Brown DG, Visse R, Sandhu G, Davies A, Rizkallah PJ, Melitz C, Summers WC, Sanderson MR: Crystal structures of the thymidine kinase from herpes simplex virus type-1 in complex with deoxythymidine and ganciclovir. Nat Struct Biol. 1995 Oct;2(10):876-81. [PubMed Link Image]
  4. Wild K, Bohner T, Aubry A, Folkers G, Schulz GE: The three-dimensional structure of thymidine kinase from herpes simplex virus type 1. FEBS Lett. 1995 Jul 17;368(2):289-92. [PubMed Link Image]
  5. Wild K, Bohner T, Folkers G, Schulz GE: The structures of thymidine kinase from herpes simplex virus type 1 in complex with substrates and a substrate analogue. Protein Sci. 1997 Oct;6(10):2097-106. [PubMed Link Image]
  6. Champness JN, Bennett MS, Wien F, Visse R, Summers WC, Herdewijn P, de Clerq E, Ostrowski T, Jarvest RL, Sanderson MR: Exploring the active site of herpes simplex virus type-1 thymidine kinase by X-ray crystallography of complexes with aciclovir and other ligands. Proteins. 1998 Aug 15;32(3):350-61. [PubMed Link Image]
  7. Bennett MS, Wien F, Champness JN, Batuwangala T, Rutherford T, Summers WC, Sun H, Wright G, Sanderson MR: Structure to 1.9 A resolution of a complex with herpes simplex virus type-1 thymidine kinase of a novel, non-substrate inhibitor: X-ray crystallographic comparison with binding of aciclovir. FEBS Lett. 1999 Jan 25;443(2):121-5. [PubMed Link Image]
Target 4 Drug References
  1. Bennett MS, Wien F, Champness JN, Batuwangala T, Rutherford T, Summers WC, Sun H, Wright G, Sanderson MR: Structure to 1.9 A resolution of a complex with herpes simplex virus type-1 thymidine kinase of a novel, non-substrate inhibitor: X-ray crystallographic comparison with binding of aciclovir. FEBS Lett. 1999 Jan 25;443(2):121-5. [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.