1UJN

Crystal structure of dehydroquinate synthase from Thermus thermophilus HB8

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.236 
  • R-Value Work: 0.202 
  • R-Value Observed: 0.203 

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This is version 1.3 of the entry. See complete history. 


Literature

Crystal structure of dehydroquinate synthase from Thermus thermophilus HB8 showing functional importance of the dimeric state.

Sugahara, M., Nodake, Y., Sugahara, M., Kunishima, N.

(2005) Proteins 58: 249-252


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
dehydroquinate synthase
A, B
348Thermus thermophilus HB8Mutation(s): 0 
EC: 4.2.3.4
UniProt
Find proteins for P83703 (Thermus thermophilus)
Explore P83703 
Go to UniProtKB:  P83703
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP83703
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.236 
  • R-Value Work: 0.202 
  • R-Value Observed: 0.203 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 63.403α = 90
b = 71.787β = 99.44
c = 71.636γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
SCALEPACKdata scaling
AMoREphasing
CNSrefinement
HKL-2000data reduction

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2003-09-02
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Source and taxonomy, Version format compliance
  • Version 1.3: 2023-10-25
    Changes: Data collection, Database references, Refinement description