2DSY

Crystal structure of TTHA0281 from thermus thermophilus HB8

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.232 
  • R-Value Work: 0.183 
  • R-Value Observed: 0.185 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history. 


Literature

Structure of a UPF0150-family protein from Thermus thermophilus HB8

Okazaki, N., Kumei, M., Manzoku, M., Kuramitsu, S., Shirouzu, M., Shinkai, A., Yokoyama, S.

(2007) Acta Crystallogr Sect F Struct Biol Cryst Commun 63: 173-177

  • DOI: https://doi.org/10.1107/S1744309107006070
  • Primary Citation of Related Structures:  
    2DSY

  • PubMed Abstract: 

    TTHA0281 is a hypothetical protein from Thermus thermophilus HB8 that belongs to an uncharacterized protein family, UPF0150, in the Pfam database and to COG1598 in the National Center for Biotechnology Information Database of Clusters of Orthologous Groups. The X-ray crystal structure of the protein was determined by a multiple-wavelength anomalous dispersion technique and was refined at 1.9 A resolution to a final R factor of 18.5%. The TTHA0281 monomer adopts an alpha-beta-beta-beta-alpha fold and forms a homotetramer. Based on the properties and functions of structural homologues of the TTHA0281 monomer, the TTHA0281 protein is speculated to be involved in RNA metabolism, including RNA binding and cleavage.

    • Organizational Affiliation: 

    RIKEN SPring-8 Center, Harima Institute, Sayo, Hyogo 679-5148, Japan.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Hypothetical protein TTHA0281
A, B, C, D
87Thermus thermophilusMutation(s): 3 
UniProt
Find proteins for Q5SLL2 (Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8))
Explore Q5SLL2 
Go to UniProtKB:  Q5SLL2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ5SLL2
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A, B, C, D
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.232 
  • R-Value Work: 0.183 
  • R-Value Observed: 0.185 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 38.996α = 90
b = 62.743β = 104.31
c = 65.724γ = 90
Software Package:
Software NamePurpose
SOLVEphasing
REFMACrefinement
HKL-2000data reduction
SCALEPACKdata scaling

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-03-27
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance