5KKU

Crystal structure of an N-terminal dehydratase from difficidin assembly line

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.22 Å
  • R-Value Free: 0.248 
  • R-Value Work: 0.217 
  • R-Value Observed: 0.219 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history. 


Literature

A Dehydratase Provides Insights into Split Bimodules and Polypeptide Docking in trans-AT Polyketide Synthases

Zeng, J., Keatinge-Clay, A.T.

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Polyketide synthase type I
A, B, C, D
300Bacillus amyloliquefaciensMutation(s): 0 
Gene Names: difJ
UniProt
Find proteins for Q1RS44 (Bacillus amyloliquefaciens)
Explore Q1RS44 
Go to UniProtKB:  Q1RS44
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ1RS44
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.22 Å
  • R-Value Free: 0.248 
  • R-Value Work: 0.217 
  • R-Value Observed: 0.219 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 41.355α = 90.2
b = 73.981β = 90.08
c = 94.178γ = 90.66
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
PDB_EXTRACTdata extraction

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-12-21
    Type: Initial release
  • Version 1.1: 2017-08-23
    Changes: Data collection, Refinement description
  • Version 1.2: 2023-09-27
    Changes: Data collection, Database references, Refinement description