1R69

STRUCTURE OF THE AMINO-TERMINAL DOMAIN OF PHAGE 434 REPRESSOR AT 2.0 ANGSTROMS RESOLUTION


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Observed: 0.193 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structure of the amino-terminal domain of phage 434 repressor at 2.0 A resolution.

Mondragon, A.Subbiah, S.Almo, S.C.Drottar, M.Harrison, S.C.

(1989) J Mol Biol 205: 189-200

  • DOI: https://doi.org/10.1016/0022-2836(89)90375-6
  • Primary Citation of Related Structures:  
    1R69

  • PubMed Abstract: 

    The crystal structure of the amino-terminal domain of phage 434 repressor has been solved using molecular replacement methods and refined to an R-factor of 19.3% against data to 2.0 A resolution. The protein comprises five short alpha-helices. Two of these form a helix-turn-helix motif, very similar to those found in related proteins. The protein is remarkably similar to the Cro protein from the same phage.


  • Organizational Affiliation

    Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
REPRESSOR PROTEIN CI69Phage 434Mutation(s): 0 
UniProt
Find proteins for P16117 (Enterobacteria phage 434)
Explore P16117 
Go to UniProtKB:  P16117
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP16117
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Observed: 0.193 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 32.8α = 90
b = 37.5β = 90
c = 44.6γ = 90
Software Package:
Software NamePurpose
PROLSQrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1989-10-15
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-14
    Changes: Data collection, Database references, Other