1JHG

TRP REPRESSOR MUTANT V58I


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.30 Å
  • R-Value Free: 0.172 
  • R-Value Observed: 0.122 

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Ligand Structure Quality Assessment 


This is version 1.5 of the entry. See complete history


Literature

An atomic view of the L-tryptophan binding site of trp repressor.

Lawson, C.L.

(1996) Nat Struct Biol 3: 986-987


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TRP OPERON REPRESSOR101Escherichia coliMutation(s): 1 
UniProt
Find proteins for P0A881 (Escherichia coli (strain K12))
Explore P0A881 
Go to UniProtKB:  P0A881
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0A881
Sequence Annotations
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  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.30 Å
  • R-Value Free: 0.172 
  • R-Value Observed: 0.122 
  • Space Group: P 21 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 53.536α = 90
b = 32.789β = 90
c = 53.385γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
SHELXL-93model building
SHELXL-93refinement
SHELXL-93phasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

  • Released Date: 1997-03-12 
  • Deposition Author(s): Lawson, C.L.

Revision History  (Full details and data files)

  • Version 1.0: 1997-03-12
    Type: Initial release
  • Version 1.1: 2008-03-03
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2014-05-21
    Changes: Database references
  • Version 1.4: 2021-11-03
    Changes: Database references, Derived calculations
  • Version 1.5: 2024-02-07
    Changes: Data collection