4BVY

Crystal structure of the AIMP3-MRS N-terminal domain complex


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.99 Å
  • R-Value Free: 0.218 
  • R-Value Work: 0.189 
  • R-Value Observed: 0.190 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

Crystal Structure of the Aimp3-Mrs N-Terminal Domain Complex

Cho, H.Y.Seo, W.W.Cho, H.J.Kang, B.S.

To be published.

Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
METHIONINE--TRNA LIGASE, CYTOPLASMIC232Homo sapiensMutation(s): 0 
EC: 6.1.1.10
UniProt & NIH Common Fund Data Resources
Find proteins for P56192 (Homo sapiens)
Explore P56192 
Go to UniProtKB:  P56192
PHAROS:  P56192
GTEx:  ENSG00000166986 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP56192
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
EUKARYOTIC TRANSLATION ELONGATION FACTOR 1 EPSILON-1186Homo sapiensMutation(s): 1 
UniProt & NIH Common Fund Data Resources
Find proteins for O43324 (Homo sapiens)
Explore O43324 
Go to UniProtKB:  O43324
PHAROS:  O43324
GTEx:  ENSG00000124802 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO43324
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.99 Å
  • R-Value Free: 0.218 
  • R-Value Work: 0.189 
  • R-Value Observed: 0.190 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 43.175α = 90
b = 71.25β = 104.83
c = 64.338γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
PHENIXphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-07-16
    Type: Initial release