PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A FARNESYLATED K-RAS4B PEPTIDE PRODUCT
1KZP
Primary Citation
 
 
  •   Molecular Description Hide
    Classification: Transferase/transferase Substrate
    Structure Weight: 94512.08
    Molecule: Protein Farnesyltransferase alpha subunit
    Polymer: 1 Type: protein Length: 377
    Chains: A
    EC#: 2.5.1.58    2.5.1.59   
    Organism: Rattus norvegicus
    Gene Name: Fnta
    UniProtKB: Protein Feature View | Search PDB | Q04631  
    Molecule: Protein Farnesyltransferase beta subunit
    Polymer: 2 Type: protein Length: 437
    Chains: B
    EC#: 2.5.1.58   
    Organism: Rattus norvegicus
    Gene Name: Fntb
    UniProtKB: Protein Feature View | Search PDB | Q02293  
    Molecule: Farnesylated K-Ras4B peptide product
    Polymer: 3 Type: protein Length: 11
    Chains: C
     
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  •   Source Hide
    Polymer: 1
    Scientific Name: Rattus norvegicus   Taxonomy   Common Name: Norway rat Expression System: Spodoptera frugiperda  
    Polymer: 2
    Scientific Name: Rattus norvegicus   Taxonomy   Common Name: Norway rat Expression System: Spodoptera frugiperda  
    Polymer: 3
    Scientific Name: Synthetic construct   Taxonomy    
     
  •   Related PDB Entries Hide
    Identifier Details
    1D8D   Protein farnesyltransferase complexed with a K-Ras4B peptide substrate and farnesyl diphosphate analog 
    1FT1   Unliganded protein farenesyltransferase 
    1FT2   protein farnesyltransferase complexed with the farnesyl diphosphate substrate 
    1JCQ   Crystal Structure Of Human Protein Farnesyltransferase Complexed With Farnesyl Diphosphate and The Peptidomimetic Inhibitor L-739,750 
    1kzo   CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH FARNESYLATED K-RAS4B PEPTIDE PRODUCT AND FARNESYL DIPHOSPHATE SUBSTRATE BOUND SIMULTANEOUSLY 
    1kzr   Transition state model of the protein farnesyltransferase reaction based on crystal structures of protein farnesyltransferase with bound substrates and products 
     
  •   Ligand Chemical Component Hide
     
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  •   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:   Long, S.B.,  Casey, P.J.,  Beese, L.S.

    Deposition:   2002-02-07
    Release:   2002-10-16
    Last Modified (REVDAT):   2011-07-13
     
  •   Revision History    Hide
    Mouse over text for details
    2011-07-13
    Polymer description
    2011-07-13
    Version format compliance
    2011-07-13
    Atom nomenclature
    2011-07-13
    Binding sites and description
    2011-07-13
    Non-polymer description
    2011-07-13
    Function and keywords
    2011-07-13
    Linkage
    2011-07-13
    Sequence database correspondence
     
  •   Experimental Details Hide
    Method:   X-RAY DIFFRACTION
    Exp. Data:
      Structure Factors
    EDS  
    Resolution[Å]:   2.10
    R-Value: 0.164 (obs.)
    R-Free: 0.202
    Space Group: P 61
    Unit Cell:
      Length [Å] Angles [°]
    a = 171.24 α = 90.00 
    b = 171.24 β = 90.00 
    c = 69.36 γ = 120.00