Return to main results Retrieve Phyre Job Id

Job DescriptionP09832
Confidence98.62%DateThu Jan 5 11:02:29 GMT 2012
Rank250Aligned Residues72
% Identity28%Templated1nhpa2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.00

  Insertion relative to template
  Deletion relative to template
  Catalytic residue from the CSA
 
Detailed help on interpreting your alignment


   142.......150.........160.........170.........180.........190.........200.........210.........220.
Predicted Secondary structure 































Query SS confidence 















































































Query Sequence  VKQTGKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEVGR
Query Conservation      
















  
   
  


 

    

 
  


                   

       
  
Alig confidence 








































........






























Template Conservation         






  
 
 
  
   
  
 

      
........               
   

       
  
Template Sequence  VDPEVNNVVVIGSGYIGIEAAEAFAKAGKKVTVIDILDRPL. . . . . . . . GVYLDKEFTDVLTEEMEANNITIATGETVER
Template Known Secondary structure  T
TT



STT
SSSSTT........TTT

TTTS

Template Predicted Secondary structure 
















........










Template SS confidence 















































































   145....150.........160.........170.........180..... ....190.........200.........210......
 
Download:Text version

No model constructed - rank, confidence too low




Phyre is for academic use only

Please cite: Protein structure prediction on the web: a case study using the Phyre server
Kelley LA and Sternberg MJE. Nature Protocols 4, 363 - 371 (2009) [pdf] [Import into BibTeX]
 
© Structural Bioinformatics Group, Imperial College, London
Lawrence Kelley, Benjamin Jefferys 
Disclaimer
Terms and Conditions