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Job DescriptionP37127
Confidence98.95%DateThu Jan 5 11:54:48 GMT 2012
Rank230Aligned Residues89
% Identity27%Templated1d7ya2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.10

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


   325....330.........340.........350.........360.........370.........380.........390.........400
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Query Sequence  KVDKRVAIIGAGPAGLACADVLTRNGVGVTVYDRHPEIGGLLTFGIPSFKLDKSLLARRREIFSAMGIHFELNCEV. . . .
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Template Sequence  RPQSRLLIVGGGVIGLELAATARTAGVHVSLVETQPRLM. . . . . . . . SRAAPATLADFVARYHAAQGVDLRFERSVTGSV
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STT
SSSSTT........TTTS
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   143......150.........160.........170.........180. ........190.........200.........210....
 
   401........410.........420.
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Query Sequence  . GKDVSLDSLLEQYDAVFVGVG
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Template Sequence  DGVVLLDDGTRIAADMVVVGIG
Template Known Secondary structure  TTTTS

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   215....220.........230......
 
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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]
 
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Lawrence Kelley, Benjamin Jefferys 
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