1BKB

INITIATION FACTOR 5A FROM ARCHEBACTERIUM PYROBACULUM AEROPHILUM


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.75 Å
  • R-Value Free: 0.236 
  • R-Value Work: 0.214 
  • R-Value Observed: 0.214 

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This is version 1.2 of the entry. See complete history


Literature

Structure of translation initiation factor 5A from Pyrobaculum aerophilum at 1.75 A resolution.

Peat, T.S.Newman, J.Waldo, G.S.Berendzen, J.Terwilliger, T.C.

(1998) Structure 6: 1207-1214

  • DOI: https://doi.org/10.1016/s0969-2126(98)00120-8
  • Primary Citation of Related Structures:  
    1BKB

  • PubMed Abstract: 

    Translation initiation factor 5A (IF-5A) is reported to be involved in the first step of peptide bond formation in translation, to be involved in cell-cycle regulation and to be a cofactor for the Rev and Rex transactivator proteins of human immunodeficiency virus-1 and T-cell leukemia virus I, respectively. IF-5A contains an unusual amino acid, hypusine (N-epsilon-(4-aminobutyl-2-hydroxy)lysine), that is required for its function. The first step in the post-translational modification of lysine to hypusine is catalyzed by the enzyme deoxyhypusine synthase, the structure of which has been published recently.


  • Organizational Affiliation

    Life Sciences Division Los Alamos National Laboratory Mail Stop M888, Los Alamos, New Mexico, 87545, USA peat@proi1.lanl.gov


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TRANSLATION INITIATION FACTOR 5A136Pyrobaculum aerophilumMutation(s): 0 
UniProt
Find proteins for P56635 (Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2))
Explore P56635 
Go to UniProtKB:  P56635
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP56635
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.75 Å
  • R-Value Free: 0.236 
  • R-Value Work: 0.214 
  • R-Value Observed: 0.214 
  • Space Group: I 4
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 114.13α = 90
b = 114.13β = 90
c = 32.59γ = 90
Software Package:
Software NamePurpose
CNSrefinement
SOLVEphasing
DENZOdata reduction
MOSFLMdata reduction
CCP4data scaling
CNSphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-11-04
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance