2KRB

Solution structure of EIF3B-RRM bound to EIF3J peptide


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 10 
  • Selection Criteria: structures with the least restraint violations 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

The indispensable N-terminal half of eIF3j/HCR1 co-operates with its structurally conserved binding partner eIF3b/PRT1-RRM and eIF1A in stringent AUG selection

Elantak, L.Wagner, S.Herrmannova, A.Janoskova, M.Rutkai, E.Lukavsky, P.J.Valasek, L.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Eukaryotic translation initiation factor 3 subunit B81Homo sapiensMutation(s): 0 
Gene Names: EIF3BEIF3S9
UniProt & NIH Common Fund Data Resources
Find proteins for P55884 (Homo sapiens)
Explore P55884 
Go to UniProtKB:  P55884
PHAROS:  P55884
GTEx:  ENSG00000106263 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP55884
Sequence Annotations
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  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Eukaryotic translation initiation factor 3 subunit J11Homo sapiensMutation(s): 0 
Gene Names: EIF3JEIF3S1PRO0391
UniProt & NIH Common Fund Data Resources
Find proteins for O75822 (Homo sapiens)
Explore O75822 
Go to UniProtKB:  O75822
PHAROS:  O75822
GTEx:  ENSG00000104131 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO75822
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 10 
  • Selection Criteria: structures with the least restraint violations 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-01-05
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2022-03-16
    Changes: Data collection, Database references, Derived calculations