4ZAJ

2.2 Angstrom Crystal Structure of a Human Arginyl-tRNA Synthetase

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.22 Å
  • R-Value Free: 0.264 
  • R-Value Work: 0.219 
  • R-Value Observed: 0.221 

wwPDB Validation   3D Report Full Report


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


Literature

2.2 Angstrom crystal structure of a human Arginyl-tRNA synthetase

Smith, A.T., Rosenzweig, A.C.

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Arginine--tRNA ligase, cytoplasmic601Homo sapiensMutation(s): 0 
Gene Names: RARS
EC: 6.1.1.19
UniProt & NIH Common Fund Data Resources
Find proteins for P54136 (Homo sapiens)
Explore P54136 
Go to UniProtKB:  P54136
PHAROS:  P54136
GTEx:  ENSG00000113643 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP54136
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.22 Å
  • R-Value Free: 0.264 
  • R-Value Work: 0.219 
  • R-Value Observed: 0.221 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 54.72α = 90
b = 61.92β = 90
c = 208.47γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
xia2data scaling
PHASERphasing
PDB_EXTRACTdata extraction
xia2data reduction

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-03-30
    Type: Initial release
  • Version 1.1: 2016-07-20
    Changes: Data collection
  • Version 1.2: 2017-11-01
    Changes: Author supporting evidence, Derived calculations
  • Version 1.3: 2023-09-27
    Changes: Data collection, Database references, Refinement description