5E3I

Crystal Structure of a Histidyl-tRNA synthetase from Acinetobacter baumannii with bound L-Histidine and ATP


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.205 
  • R-Value Work: 0.165 
  • R-Value Observed: 0.166 

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This is version 1.1 of the entry. See complete history


Literature

Crystal Structure of a Histidyl-tRNA synthetase from Acinetobacter baumannii with bound L-Histidine and ATP

SSGCIDLukacs, C.M.Dranow, D.M.Lorimer, D.Edwards, T.E.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Histidine--tRNA ligase
A, B
438Acinetobacter baumanniiMutation(s): 0 
Gene Names: hisSABUW_3376IOMTU433_3293RU84_15845
EC: 6.1.1.21
UniProt
Find proteins for B0VKR7 (Acinetobacter baumannii (strain SDF))
Explore B0VKR7 
Go to UniProtKB:  B0VKR7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupB0VKR7
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

Unit Cell:
Length ( Å )Angle ( ˚ )
a = 88.81α = 90
b = 103.07β = 90
c = 246.3γ = 90
Software Package:
Software NamePurpose
XSCALEdata scaling
PHENIXrefinement
PDB_EXTRACTdata extraction
XDSdata reduction
BALBESphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2015-11-04
    Type: Initial release
  • Version 1.1: 2023-09-27
    Changes: Data collection, Database references, Derived calculations, Refinement description