Viability of a drug-resistant HIV-1 protease mutant: structural insights for better antiviral therapy
1MT8
Primary Citation
 
 
  •   Molecular Description Hide
    Classification: Hydrolase/hydrolase Substrate
    Structure Weight: 22800.03
    Molecule: PROTEASE RETROPEPSIN
    Polymer: 1 Type: protein Length: 99
    Chains: A, B
    EC#: 3.4.23.16   
    Mutation: Q7K, D25N, L63P, V82A
    Organism: Human immunodeficiency virus 1
    Gene Name: gag-pol
    UniProtKB: Protein Feature View | Search PDB | P03369  
    Molecule: Capsid-p2 substrate peptide of HIV-1 Gag polyprotein
    Polymer: 2 Type: protein Length: 10
    Chains: P
    Organism: HIV-1 CRF04_cpx
    Gene Name: gag
    UniProtKB: Protein Feature View | Search PDB | Q9YX54  
     
  •   Structure Validation Hide

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  •   Related Citations in PDB Entry (REMARK 1) Hide
     
  •   Source Hide
    Polymer: 1
    Scientific Name: Human immunodeficiency virus 1   Taxonomy   Expression System: Escherichia coli  
    Polymer: 2
    Scientific Name: Synthetic construct (HIV-1 CRF04_cpx)   Taxonomy    
     
  •   Related PDB Entries Hide
    Identifier Details
    1KJ4   Inactive wild-type HIV-1 protease (D25N) complexed with its Gag substrate peptide MA-CA. 
    1MT7    
    1MT9    
    1MTB    
    1MTR   HIV-1 PROTEASE COMPLEXED WITH A CYCLIC PHE-ILE-VAL PEPTIDOMIMETIC INHIBITOR 
     
  •   Ligand Chemical Component Hide
    Identifier Formula Name View Interactions
    ACT
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    ACT C2 H3 O2
    ACETATE ION
     
  •   External Domain Annotations Hide
     
  •   Structural Biology Knowledgebase Data Hide
     
 
Data in orange boxes are gathered from external resources (when available).
  Biological Assembly       
Biological assembly 1 assigned by authors and generated by PISA (software)
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  •   Deposition Summary Hide
    Authors:   Prabu-Jeyabalan, M.,  Nalivaika, E.A.,  King, N.M.,  Schiffer, C.A.

    Deposition:   2002-09-20
    Release:   2003-01-07
    Last Modified (REVDAT):   2009-02-24
     
  •   Revision History    Hide
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    2011-07-13
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  •   Experimental Details Hide
    Method:   X-RAY DIFFRACTION
    Exp. Data:
    N/A
    Resolution[Å]:   2.15
    R-Value: 0.208 (obs.)
    R-Free: 0.243
    Space Group: P 21 21 21
    Unit Cell:
      Length [Å] Angles [°]
    a = 51.56 α = 90.00 
    b = 59.38 β = 90.00 
    c = 61.87 γ = 90.00