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Summary Structural Experimental Function Sequence Neighbor Download Link


<Asymmetric unit>

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( jV3 / Jmol ) *1
PDB ID3k4v  sequence information (FASTA format)   
DescriptorHIV-1 Protease (E.C.3.4.23.16)
TitleNew crystal form of HIV-1 Protease/Saquinavir structure reveals carbamylation of N-terminal proline
Functional KeywordsHIV-1 PROTEASE, SAQUINAVIR, SUBSTRATE ANALOG, HYDROLASE, CARBAMYLATION, AIDS, Aspartyl protease, Capsid maturation, Capsid protein, Cell membrane, Cytoplasm, DNA integration, DNA recombination, DNA-directed DNA polymerase, Endonuclease, Lipoprotein, Magnesium, Membrane, Metal-binding, Multifunctional enzyme, Myristate, Nuclease, Nucleotidyltransferase, Nucleus, Phosphoprotein, Protease, Ribosomal frameshifting, RNA-binding, RNA-directed DNA polymerase, Transferase, Viral nucleoprotein, Virion, Zinc, Zinc-finger
Biological sourceHuman immunodeficiency virus type 1 (HIV-1)
Cellular location [UNP - P03366] Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential)
Total number of polymer chains4
Total molecular weight44706.7 (the details in Structural Details Page)
AuthorsOlajuyigbe, F.M. , Demitri, N. , Ajele, J.O. , Maurizio, E. , Randaccio, L. , Geremia, S. (deposition date : 2009-10-06, release date : 2010-06-09)
Primary citationOlajuyigbe, F.M. , Demitri, N. , Ajele, J.O. , Maurizio, E. , Randaccio, L. , Geremia, S.
New crystal form of HIV-1 Protease/Saquinavir structure reveals carbamylation of N-terminal proline
ACS Med.Chem.Lett., : - , 2010.  (DOI: 10.1021/ml100046d)
Experimental methodX-RAY DIFFRACTION ( 1.39[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P03366 ) , eF-site , KEGG ( EC 3.4.23.16 ) , PISA