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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:06:42
Primary Accession Number DB00224
Secondary Accession Number
  • APRD00069
Name Indinavir
Drug Type
  • Approved
  • Small Molecule
Description A potent and specific HIV protease inhibitor that appears to have good oral bioavailability. [PubChem]
Synonyms
  1. Compound J
  2. Indinavir sulfate
Brand Names
  1. Crixivan
Brand Mixtures Not Available
Chemical IUPAC Name (2S)-N-tert-butyl-1-[(2S,4R)-2-hydroxy-5-[[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]amino]-5-oxo-4-(phenylmethyl)pentyl]-4-(pyridin-3-ylmethyl)piperazine-2-carboxamide
Chemical Formula C36H47N5O4
Chemical Structure Structure
CAS Registry Number 150378-17-9
InChI Identifier InChI=1/C36H47N5O4/c1-36(2,3)39-35(45)31-24-40(22-26-12-9-15-37-21-26)16-17-41(31)23-29(42)19-28(18-25-10-5-4-6-11-25)34(44)38-33-30-14-8-7-13-27(30)20-32(33)43/h4-15,21,28-29,31-33,42-43H,16-20,22-24H2,1-3H3,(H,38,44)(H,39,45)/t28-,29+,31+,32-,33+/m1/s1/f/h38-39H
InChI Key CBVCZFGXHXORBI-WCUGGTCDDP
KEGG Drug Not Available
KEGG Compound C07051 Link Image
PubChem Compound 5362440 Link Image
PubChem Substance 197165 Link Image
ChEBI ID 5898 Link Image
PharmGKB ID PA449977 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02229161 Link Image
RxList Link http://www.rxlist.com/cgi/generic2/indinav.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Indinavir Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference J. P. Vacca et al U.S.pat. 5,413,999 (1995)
Average Molecular Weight 613.7895
Monoisotopic Molecular Weight 613.3628
State Solid
Melting Point 167.5-168 oC
Experimental Water Solubility 0.015 mg/ml Source: PhysProp
Predicted Water Solubility 4.82e-02 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 2.9 Source: PhysProp
Predicted LogP 3.26 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -4.11 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 1ODW Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES CC(C)(C)NC(=O)[C@@H]1CN(CCN1C[C@@H](O)C[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H]1[C@H](O)CC2=CC=CC=C12)CC1=CN=CC=C1
Canonical SMILES CC(C)(C)NC(=O)C1CN(CCN1CC(O)CC(CC1=CC=CC=C1)C(=O)NC1C(O)CC2=CC=CC=C12)CC1=CN=CC=C1
Drug Category
  • Anti-HIV Agents
  • HIV Protease Inhibitors
ATC Codes
AHFS Codes
  • 08:18.08.08
Indication For the treatment of HIV infection.
Pharmacology Indinavir is a protease inhibitor with activity against Human Immunodeficiency Virus Type 1 (HIV-1). Protease inhibitors block the part of HIV called protease. HIV-1 protease is an enzyme required for the proteolytic cleavage of the viral polyprotein precursors into the individual functional proteins found in infectious HIV-1. Indinavir binds to the protease active site and inhibits the activity of the enzyme. This inhibition prevents cleavage of the viral polyproteins resulting in the formation of immature non-infectious viral particles. Protease inhibitors are almost always used in combination with at least two other anti-HIV drugs.
Mechanism of Action Indinavir inhibits the HIV viral proteinase enzyme which prevents cleavage of the gag-pol polyprotein, resulting in noninfectious, immature viral particles.
Absorption Rapidly absorbed
Toxicity Symptoms of overdose include myocardial infarction and angina pectoris.
Protein Binding 60%
Biotransformation Hepatic. Seven metabolites have been identified, one glucuronide conjugate and six oxidative metabolites. In vitro studies indicate that cytochrome P-450 3A4 (CYP3A4) is the major enzyme responsible for formation of the oxidative metabolites.
Half Life 1.8 (± 0.4) hours
Dosage Forms
Form Route
Capsule Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Acenocoumarol The protease inhibitor increases the anticoagulant effect
Alprazolam The protease inhibitor increases the effect of the benzodiazepine
Aluminium The antacid decreases the absorption of indinavir
Amiodarone Indinavir increases the effect and toxicity of amiodarone
Anisindione The protease inhibitor increases the anticoagulant effect
Astemizole Increased risk of cardiotoxicity and arrhythmias
Atazanavir Increased risk of hyperbilirubinemia with this association
Atorvastatin Increases the effect and toxicity of atorvastatin
Bismuth The antacid decreases the absorption of indinavir
Calcium The antacid decreases the absorption of indinavir
Carbamazepine Indinavir increases the effect and toxicity of carbamazepine
Chlordiazepoxide The protease inhibitor increases the effect of the benzodiazepine
Cisapride Increased risk of cardiotoxicity and arrhythmias
Clarithromycin Clarithromycin increases the effect and toxicity of indinavir
Clonazepam The protease inhibitor increases the effect of the benzodiazepine
Clorazepate The protease inhibitor increases the effect of the benzodiazepine
Cyclosporine The protease inhibitor increases the effect of cyclosporine
Delavirdine Delavirdine increases the effect of indinavir
Diazepam The protease inhibitor increases the effect of the benzodiazepine
Dicumarol The protease inhibitor increases the anticoagulant effect
Dihydroergotamine Increases the effect and toxicity of the ergot derivative
Efavirenz Efavirenz decreases the effect of indinavir
Ergotamine Increases the effect and toxicity of the ergot derivative
Erlotinib This CYP3A4 inhibitor increases levels/toxicity of erlotinib
Esomeprazole Omeprazole decreases the absorption of indinavir
Estazolam The protease inhibitor increases the effect of the benzodiazepine
Fentanyl The protease inhibitor increases the effect and toxicity of fentanyl
Flurazepam The protease inhibitor increases the effect of the benzodiazepine
Fusidic Acid Increases the effect and toxicity of fusidic acid
Halazepam The protease inhibitor increases the effect of the benzodiazepine
Ketoconazole Ketoconazole increases the efefct of indinavir
Lansoprazole Omeprazole decreases the absorption of indinavir
Magnesium The antacid decreases the absorption of indinavir
Magnesium oxide The antacid decreases the absorption of indinavir
Midazolam The protease inhibitor increases the effect of the benzodiazepine
Omeprazole Omeprazole decreases the absorption of indinavir
Pantoprazole Omeprazole decreases the absorption of indinavir
Pimozide The protease inhibitor increases the effect and toxicity of pimozide
Prazepam The protease inhibitor increases the effect of the benzodiazepine
Quazepam The protease inhibitor increases the effect of the benzodiazepine
Quinupristin This combination presents an increased risk of toxicity
Rabeprazole Omeprazole decreases the absorption of indinavir
Ranolazine Increased levels of ranolazine - risk of toxicity
Rifabutin Rifabutin decreases the effect of indinavir
Rifampin Rifampin decreases the effect of indinavir
Risperidone Increased risk of extrapyramidal symptoms
Saquinavir Possible antagonism of action
Sildenafil The protease inhibitor increases the effect and toxicity of sildenafil
St. John's Wort St. John's Wort decreases the effect of indinavir
Sunitinib Possible increase in sunitinib levels
Tacrolimus Increases the effect and toxicity of tacrolimus
Terfenadine Increased risk of cardiotoxicity and arrhythmias
Trazodone This strong CYP3A4 inhibitor increases the effect and toxicity of trazodone
Triazolam The protease inhibitor increases the effect of the benzodiazepine
Vardenafil The protease inhibitor increases the effect and toxicity of vardenafil
Vitamin C Vitamin C decreases indinavir levels
Warfarin The protease inhibitor increases the anticoagulant effect
Food Interactions
  • Avoid excessive or chronic alcohol use.
  • Avoid taking with grapefruit juice
  • Take on empty stomach: 1 hour before or 2 hours after meals.
  • Take with a full glass of water.
Pathways Not Available
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
Organisms Affected
  • Human Immunodeficiency Virus
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 3A5 (CYP3A5)
  2. Cytochrome P450 3A4 (CYP3A4)
Targets
  1. Gag-Pol polyprotein
  2. HIV-1 protease
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 3A5 (CYP3A5)
Enzyme 1 Gene Name CYP3A5
Enzyme 1 SwissProt ID P20815 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P20815|CP3A5_HUMAN Cytochrome P450 3A5 
MDLIPNLAVETWLLLAVSLVLLYLYGTRTHGLFKRLGIPGPTPLPLLGNVLSYRQGLWKF
DTECYKKYGKMWGTYEGQLPVLAITDPDVIRTVLVKECYSVFTNRRSLGPVGFMKSAISL
AEDEEWKRIRSLLSPTFTSGKLKEMFPIIAQYGDVLVRNLRREAEKGKPVTLKDIFGAYS
MDVITGTSFGVNIDSLNNPQDPFVESTKKFLKFGFLDPLFLSIILFPFLTPVFEALNVSL
FPKDTINFLSKSVNRMKKSRLNDKQKHRLDFLQLMIDSQNSKETESHKALSDLELAAQSI
IFIFAGYETTSSVLSFTLYELATHPDVQQKLQKEIDAVLPNKAPPTYDAVVQMEYLDMVV
NETLRLFPVAIRLERTCKKDVEINGVFIPKGSMVVIPTYALHHDPKYWTEPEEFRPERFS
KKKDSIDPYIYTPFGTGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLDTQG
LLQPEKPIVLKVDSRDGTLSGE
Phase 1 Metabolizing Enzyme 2 [top]
Enzyme 2 Name Cytochrome P450 3A4 (CYP3A4)
Enzyme 2 Gene Name CYP3A4
Enzyme 2 SwissProt ID P08684 Link Image
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 Protein Sequence >sp|P08684|CP3A4_HUMAN Cytochrome P450 3A4 (EC 1.14.13.67) 
ALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFD
MECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIA
EDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSM
DVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVF
PREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSII
FIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVN
ETLRLFPIAMRLERVCKKDVEINGMFIPKGWVVMIPSYALHRDPKYWTEPEKFLPERFSK
KNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGG
LLQPEKPVVLKVESRDGTVSGA
Drug Target 1 [top]
Target 1 ID 460
Target 1 Name Gag-Pol polyprotein
Target 1 Synonyms
  1. Pr160Gag-Pol
Target 1 Gene Name gag
Target 1 Protein Sequence >Gag-Pol polyprotein 
GARNSVLRGKKADELEKVRLRPGGKKKYRLKHIVWAANELDKFGLAESLLESKEGCQKIL
RVLDPLVPTGSENLKSLFNTVCVIWCLHAEEKVKDTEEAKKLAQRHLVAETGTAEKMPNT
SRPTAPPSGKRGNYPVQQAGGNYVHVPLSPRTLNAWVKLVEEKKFGAEVVPGFQALSEGC
TPYDINQMLNCVGDHQAAMQIIREIINEEAADWDSQHPIPGPLPAGQLRDPRGSDIAGTT
STVDEQIQWMYRPQNPVPVGNIYRRWIQIGLQKCVRKYNPTNILDIKQGPKEPFQSYVDR
FYKSLRAEQTDPAVKNWMTQTLLIQNANPDCKLVLKGLGMNPTLEEMLTACQGVGGPGQK
ARLMAEALKEAMGPSPIPFAAAQQRKAIRYWNCGKEGHSARQCRAPRRQGCWKCGKPGHI
MANCPERQAGFLRVGPTGKEASQLPRDPSPSGADTNSTSGRSSSGTVGEIYAAREKAEGA
EGETIQRGDGGLAAPRAERDTSQRGDRGLAAPQFSLWKRPVVTAYIEDQPVEVLLDTGAD
DSIVAGIELGDNYTPKIVGGIGGFINTKEYKNVEIKVLNKRVRATIMTGDTPINIFGRNI
LTALGMSLNLPVAKIEPIKVTLKPGKDGPRLKQWPLTKEKIEALKEICEKMEKEGQLEEA
PPTNPYNTPTFAIKKKDKNKWRMLIDFRELNKVTQDFTEIQLGIPHPAGLAKKKRISILD
VGDAYFSIPLHEDFRQYTAFTLPAVNNMEPGKRYIYKVLPQGWKGSPAIFQYTMRQVLEP
FRKANPDVILIQYMDDILIASDRTGLEHDKVVLQLKELLNGLGFSTPDEKFQKDPPFQWM
GCELWPTKWKLQKLQLPQKDIWTVNDIQKLVGVLNWAAQIYSGIKTKHLCRLIRGKMTLT
EEVQWTELAEAELEENKIILSQEQEGYYYQEEKELEATIQKSQGHQWTYKIHQEEKILKV
GKYAKIKNTHTNGVRLLAQVVQKIGKEALVIWGRIPKFHLPVERETWEQWWDNYWQVTWI
PEWDFVSTPPLVRLTFNLVGDPIPGAETFYTDGSCNRQSKEGKAGYVTDRGKDKVKVLEQ
TTNQQAELEVFRMALADSGPKVNIIVDSQYVMGIVAGQPTESENRIVNQIIEEMIKKEAV
YVAWVPAHKGIGGNQEVDHLVSQGIRQVLFLEKIEPAQEEHEKYHSIIKELTHKFGIPLL
VARQIVNSCAQCQQKGEAIHGQVNAEIGVWQMDYTHLEGKIIIVAVHVASGFIEAEVIPQ
ESGRQTALFLLKLASRWPITHLHTDNGPNFTSQEVKMVAWWVGIEQSFGVPYNPQSQGVV
EAMNHHLKNQISRIREQANTIETIVLMAVHCMNFKRRGGIGDMTPAERLINMITTEQEIQ
FLQRKNSNFKNFQVYYREGRDQLWKGPGELLWKGEGAVIVKVGTDIKVVPRRKAKIIRDY
GGRQELDSSPHLEGAREDGEMACPCQVPEIQNKRPRGGALCSPPQGGMGMVDLQQGNIPT
TRKKSSRNTGILEPNTRKRMALLSCSKINLVYRKVLDRCYPRLCRHPNT
Target 1 Number of Residues 1574
Target 1 Molecular Weight 174345
Target 1 Theoretical pI 9.12
Target 1 GO Classification
Function
RNA binding
transferase activity
transferase activity, transferring phosphorus-containing groups
nucleotidyltransferase activity
RNA-directed DNA polymerase activity
DNA binding
hydrolase activity, acting on ester bonds
nuclease activity
endonuclease activity
endoribonuclease activity
endoribonuclease activity, producing 5'-phosphomonoesters
ribonuclease H activity
nucleic acid binding
hydrolase activity
peptidase activity
endopeptidase activity
aspartic-type endopeptidase activity
structural molecule activity
binding
ion binding
cation binding
transition metal ion binding
zinc ion binding
catalytic activity
integrase activity
Process
DNA replication
RNA-dependent DNA replication
DNA recombination
macromolecule metabolism
protein metabolism
cellular protein metabolism
proteolysis
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
DNA metabolism
DNA integration
viral life cycle
Component
Not Available
Target 1 General Function Involved in RNA binding
Target 1 Specific Function Integrase performs the integration of the newly synthesized dsDNA copy of the viral genome into the host chromosome. The integrated DNA is called provirus
Target 1 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 1 Reactions
  • deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 1332356 Link Image
Target 1 UniProtKB/Swiss-Prot ID P18096 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name POL_HV2BE Link Image
Target 1 PDB ID 1MU2 Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Nucleus. Cytoplasm (By similarity). Following virus entry, the nuclear localization signal (NLS) of
Target 1 Gene Sequence >2892 bp 
ATGACAGGAGATACCCCAATCAACATCTTTGGCAGAAATATTCTGACAGCCTTAGGCATG
TCATTAAATTTACCAGTTGCCAAGATAGAGCCAATAAAAGTAACATTGAAGCCAGGGAAA
GATGGACCAAGGCTGAAACAATGGCCCCTAACAAAAGAGAAAATAGAAGCACTAAAAGAG
ATCTGTGAAAAAATGGAAAAAGAGGGCCAGCTAGAAGAGGCACCTCCAACTAATCCTTAT
AATACCCCCACATTTGCAATTAAGAAAAAGGACAAGAACAAATGGAGGATGCTGATAGAT
TTTAGAGAACTAAATAAGGTGACTCAAGATTTCACAGAAATTCAGCTAGGAATTCCACAC
CCGGCAGGACTAGCCAAAAAGAAAAGGATCTCTATATTAGATGTAGGGGATGCCTATTTT
TCCATACCACTACATGAAGATTTTAGGCAGTATACTGCATTTACCCTACCAGCAGTAAAC
AATATGGAACCAGGAAAAAGATATATATATAAAGTCTTGCCACAAGGATGGAAGGGATCA
CCAGCAATTTTTCAATACACAATGAGGCAAGTCTTAGAACCTTTCAGAAAAGCAAACCCA
GATGTCATTCTCATCCAGTACATGGATGATATCTTAATAGCTAGTGACAGGACAGGTTTA
GAGCATGACAAAGTGGTCCTGCAGCTAAAAGAACTTCTAAATGGCCTAGGGTTTTCTACT
CCAGATGAGAAGTTCCAAAAAGACCCTCCATTTCAATGGATGGGCTGTGAACTATGGCCA
ACTAAATGGAAGCTGCAGAAACTACAACTGCCCCAGAAAGACATATGGACAGTCAATGAC
ATCCAAAAGCTAGTGGGAGTCTTAAATTGGGCGGCACAAATCTATTCAGGAATAAAAACC
AAACACTTATGTAGACTAATTAGAGGAAAAATGACACTCACAGAAGAAGTGCAGTGGACA
GAACTAGCAGAAGCAGAGCTAGAAGAAAACAAAATTATCTTGAGCCAGGAACAAGAAGGA
TATTATTACCAAGAAGAAAAAGAATTAGAGGCAACAATCCAAAAAAGCCAAGGACATCAA
TGGACATACAAAATACACCAGGAAGAGAAAATCCTAAAAGTAGGAAAGTATGCAAAGATA
AAAAATACCCATACCAATGGGGTCAGATTACTAGCACAGGTAGTTCAGAAAATAGGAAAA
GAGGCACTAGTCATTTGGGGACGGATACCAAAATTTCACCTGCCAGTGGAGAGAGAGACC
TGGGAGCAGTGGTGGGATAACTACTGGCAAGTGACATGGATCCCAGAGTGGGACTTTGTA
TCTACCCCACCACTGGTCAGGTTAACATTTAACCTAGTAGGAGATCCTATACCAGGCGCA
GAGACCTTCTACACAGATGGATCATGCAATAGACAGTCAAAAGAGGGAAAAGCAGGATAT
GTAACAGATAGAGGAAAAGACAAAGTAAAAGTATTAGAACAAACTACCAATCAGCAGGCA
GAATTAGAAGTCTTTCGGATGGCACTGGCAGACTCAGGCCCAAAGGTTAATATCATAGTA
GATTCACAGTATGTAATGGGGATAGTAGCAGGCCAGCCAACAGAGTCAGAAAATAGAATA
GTGAACCAGATCATAGAAGAAATGATAAAGAAGGAAGCAGTCTATGTTGCATGGGTCCCA
GCCCATAAAGGCATAGGAGGAAACCAGGAAGTAGACCATTTAGTAAGTCAAGGCATCAGA
CAAGTATTATTCCTGGAAAAGATAGAGCCCGCTCAAGAGGAACATGAAAAATATCATAGC
ATTATAAAAGAACTAACCCATAAATTTGGAATACCCCTTCTAGTAGCAAGACAGATAGTA
AACTCATGTGCCCAATGCCAACAGAAAGGAGAAGCCATACATGGGCAAGTAAATGCAGAA
ATAGGCGTTTGGCAAATGGACTACACACACTTAGAAGGAAAAATCATTATAGTAGCAGTA
CATGTTGCAAGTGGATTCATAGAAGCAGAAGTCATCCCACAGGAATCAGGAAGGCAGACA
GCACTCTTCCTATTAAAACTGGCCAGTAGGTGGCCAATAACGCACTTGCACACAGACAAT
GGCCCCAACTTCACTTCACAGGAAGTGAAGATGGTGGCATGGTGGGTAGGTATAGAACAA
TCCTTTGGAGTACCTTACAACCCACAAAGCCAGGGAGTAGTAGAAGCAATGAATCACCAC
CTAAAGAATCAGATAAGTAGAATTAGAGAACAGGCAAATACAATAGAAACAATAGTACTG
ATGGCAGTTCATTGCATGAATTTTAAAAGAAGGGGAGGAATAGGGGATATGACCCCAGCA
GAAAGACTAATCAACATGATTACCACAGAACAAGAAATACAATTCCTCCAAAGAAAAAAT
TCAAATTTTAAAAATTTCCAGGTCTATTACAGAGAAGGCAGAGATCAGCTGTGGAAAGGA
CCTGGTGAACTACTGTGGAAGGGAGAAGGAGCAGTCATAGTCAAGGTAGGGACAGACATA
AAAGTAGTACCAAGAAGGAAGGCCAAGATTATCAGGGACTATGGAGGAAGACAGGAACTG
GATAGTAGTCCCCACCTGGAGGGTGCCAGGGAGGATGGAGAAATGGCATGCCCTTGTCAA
GTACCTGAAATACAGAACAAAAGACCTAGAGGAGGTGCGCTATGTTCCCCACCACAAGGT
GGGATGGGCATGGTGGACTTGCAGCAGGGTAATATTCCCACTACAAGGAAAAAGTCATCT
AGAAATACAGGCATATTGGAACCTAACACCAGAAAAAGGATGGCTCTCCTCTCATGCAGT
AAGATTAACCTGGTATACAGAAAAGTTCTGGACAGATGTTACCCCAGACTGTGCAGACAT
CCTAATACATAG
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 Not Available
Target 1 Locus Not Available
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Kirchhoff F, Jentsch KD, Bachmann B, Stuke A, Laloux C, Luke W, Stahl-Hennig C, Schneider J, Nieselt K, Eigen M, et al.: A novel proviral clone of HIV-2: biological and phylogenetic relationship to other primate immunodeficiency viruses. Virology. 1990 Jul;177(1):305-11. [PubMed Link Image]
  2. Turner BG, Summers MF: Structural biology of HIV. J Mol Biol. 1999 Jan 8;285(1):1-32. [PubMed Link Image]
Target 1 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]
  3. Barry M, Gibbons S, Back D, Mulcahy F: Protease inhibitors in patients with HIV disease. Clinically important pharmacokinetic considerations. Clin Pharmacokinet. 1997 Mar;32(3):194-209. [PubMed Link Image]
  4. Melnick L, Yang SS, Rossi R, Zepp C, Heefner D: An Escherichia coli expression assay and screen for human immunodeficiency virus protease variants with decreased susceptibility to indinavir. Antimicrob Agents Chemother. 1998 Dec;42(12):3256-65. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 731
Target 2 Name HIV-1 protease
Target 2 Synonyms
  1. Fragment
Target 2 Gene Name HIV-1 protease
Target 2 Protein Sequence >HIV-1 protease 
PQVTLWQRPIVTIKIGGQLKEALLDTGADDTVLEEMSLPGKWKPKMIGGIGGFIKVRQYD
QVSIEICGHKAIGTVLIGPTPVNIIGRNLLTQLGCTLNF
Target 2 Number of Residues 100
Target 2 Molecular Weight 10725
Target 2 Theoretical pI 8.77
Target 2 GO Classification
Function
catalytic activity
hydrolase activity
peptidase activity
endopeptidase activity
aspartic-type endopeptidase activity
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
cellular protein metabolism
proteolysis
Component
Not Available
Target 2 General Function Involved in aspartic-type endopeptidase activity
Target 2 Specific Function Not Available
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 4377614 Link Image
Target 2 UniProtKB/Swiss-Prot ID O90777 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name O90777_9PLVG Link Image
Target 2 PDB ID 1ODW Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Cytoplasmic
Target 2 Gene Sequence >297 bp 
CCTCAGGTCACTCTTTGGCAACGACCCATAGTCACAATAAAGATAGGGGGGCAACTAAAG
GAAGCTCTATTAGATACAGGAGCAGATGATACAGTATTAGAAGAAATGAGTTTGCCAGGA
AAATGGAAACCAAAAATGATAGGGGGAATTGGAGGTTTTATCAAAGTAAGACAGTATGAT
CAGGTATCCATAGAAATCTGCGGACATAAAGCTATAGGTACAGTATTAATAGGACCTACA
CCTGTCAACATAATTGGAAGGAATCTGTTGACTCAGCTTGGCTGCACTTTAAATTTT
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. Servais J, Lambert C, Fontaine E, Plesseria JM, Robert I, Arendt V, Staub T, Schneider F, Hemmer R, Burtonboy G, Schmit JC: Comparison of DNA sequencing and a line probe assay for detection of human immunodeficiency virus type 1 drug resistance mutations in patients failing highly active antiretroviral therapy. J Clin Microbiol. 2001 Feb;39(2):454-9. [PubMed Link Image]
  2. Servais J, Lambert C, Fontaine E, Plesseria JM, Robert I, Arendt V, Staub T, Schneider F, Hemmer R, Burtonboy G, Schmit JC: Variant human immunodeficiency virus type 1 proteases and response to combination therapy including a protease inhibitor. Antimicrob Agents Chemother. 2001 Mar;45(3):893-900. [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]
  3. Dandache S, Sevigny G, Yelle J, Stranix BR, Parkin N, Schapiro JM, Wainberg MA, Wu JJ: In Vitro Antiviral Activity and Cross-Resistance Profile of PL-100, a Next Generation Protease Inhibitor of Human Immunodeficiency Virus Type 1. Antimicrob Agents Chemother. 2007 Jul 16;. [PubMed Link Image]
  4. Wittayanarakul K, Hannongbua S, Feig M: Accurate prediction of protonation state as a prerequisite for reliable MM-PB(GB)SA binding free energy calculations of HIV-1 protease inhibitors. J Comput Chem. 2007 Sep 11;. [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.