1D4R

29-mer fragment of human srp rna helix 6

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.288 
  • R-Value Work: 0.264 
  • R-Value Observed: 0.264 

wwPDB Validation   3D Report Full Report


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


Literature

The 2 A structure of helix 6 of the human signal recognition particle RNA

Wild, K., Weichenrieder, O., Leonard, G.A., Cusack, S.

(1999) Structure 7: 1345-1352

  • DOI: https://doi.org/10.1016/s0969-2126(00)80024-6
  • Primary Citation of Related Structures:  
    1D4R

  • PubMed Abstract: 

    The mammalian signal recognition particle (SRP) is an essential cytoplasmic ribonucleoprotein complex involved in targeting signal-peptide-containing proteins to the endoplasmic reticulum. Assembly of the SRP requires protein SRP19 to bind first to helix 6 of the SRP RNA before the signal-peptide-recognizing protein, SRP54, can bind to helix 8 of the RNA. Helix 6 is closed by a GGAG tetraloop, which has been shown to form part of the SRP19-binding site.

    • Organizational Affiliation: 

    EMBL Grenoble Outstation, Grenoble, F-38042, France.


Macromolecules
Find similar nucleic acids by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains LengthOrganismImage
29-MER OF MODIFIED SRP RNA HELIX 629N/A
Sequence Annotations
Expand
  • Reference Sequence
Find similar nucleic acids by: 
(by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains LengthOrganismImage
29-MER OF MODIFIED SRP RNA HELIX 6
B, C
29N/A
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.288 
  • R-Value Work: 0.264 
  • R-Value Observed: 0.264 
  • Space Group: P 31 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 42.98α = 90
b = 42.98β = 90
c = 231.42γ = 120
Software Package:
Software NamePurpose
MOSFLMdata reduction
TRUNCATEdata reduction
SOLVEphasing
CNSrefinement
CCP4data scaling

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: 1999-12-02
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-07
    Changes: Data collection, Database references, Derived calculations