3L7V

Crystal structure of a hypothetical protein smu.1377c from Streptococcus mutans UA159


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.26 Å
  • R-Value Free: 0.259 
  • R-Value Work: 0.196 
  • R-Value Observed: 0.199 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

The structure of the hypothetical protein smu.1377c from Streptococcus mutans suggests a role in tRNA modification

Fu, T.-M.Liu, X.Li, L.Su, X.-D.

(2010) Acta Crystallogr Sect F Struct Biol Cryst Commun 66: 771-775

  • DOI: https://doi.org/10.1107/S1744309110018944
  • Primary Citation of Related Structures:  
    3L7V

  • PubMed Abstract: 

    Members of the Sua5_YciO_YrdC protein family are found in both eukaryotes and prokaryotes and possess a conserved alpha/beta twisted open-sheet fold. The Escherichia coli protein YrdC has been shown to be involved in modification of tRNA. The crystal structure of smu.1377c, a hypothetical protein from Streptococcus mutans, has been determined to 2.25 A resolution. From structure analysis and comparison, it is shown that smu.1377c is a member of the Sua5_YciO_YrdC family and that it may play the same role as E. coli YrdC.


  • Organizational Affiliation

    The National Laboratory of Protein Engineering and Plant Genetic Engineering, School of Life Sciences, Peking University, Beijing 100871, People's Republic of China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Putative uncharacterized protein smu.1377c295Streptococcus mutans UA159Mutation(s): 0 
Gene Names: smu.1377c
UniProt
Find proteins for Q8DTG7 (Streptococcus mutans serotype c (strain ATCC 700610 / UA159))
Explore Q8DTG7 
Go to UniProtKB:  Q8DTG7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8DTG7
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.26 Å
  • R-Value Free: 0.259 
  • R-Value Work: 0.196 
  • R-Value Observed: 0.199 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 81.9α = 90
b = 92.6β = 90
c = 40.6γ = 90
Software Package:
Software NamePurpose
MAR345dtbdata collection
SHELXSphasing
PHENIXrefinement
XDSdata reduction
XSCALEdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-07-21
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2018-05-30
    Changes: Data collection