5IX3

Crystal structure of N-acetyltransferase from Staphylococcus aureus.

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.81 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.222 
  • R-Value Observed: 0.223 

wwPDB Validation   3D Report Full Report


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


Literature

Crystal structure of N-acetyltransferase from Staphylococcus aureus.

Srivastava, P., Khandokar, Y., Forwood, J.

To be published.

Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Diamine N-acetyltransferase168Staphylococcus aureusMutation(s): 0 
Gene Names: res, speG, AL498_11440, ERS092844_02726, ERS195423_02759, R114_33, R92_33
EC: 2.3.1.57
UniProt
Find proteins for U5NVV0 (Staphylococcus aureus)
Explore U5NVV0 
Go to UniProtKB:  U5NVV0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupU5NVV0
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.81 Å
  • R-Value Free: 0.247 
  • R-Value Work: 0.222 
  • R-Value Observed: 0.223 
  • Space Group: P 6 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 107.95α = 90
b = 107.95β = 90
c = 65.23γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
iMOSFLMdata reduction
Aimlessdata scaling
PHENIXphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2017-04-05
    Type: Initial release
  • Version 1.1: 2017-04-12
    Changes: Other
  • Version 1.2: 2024-03-06
    Changes: Data collection, Database references, Derived calculations