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Job DescriptionP04391
Confidence66.96%DateThu Jan 5 10:58:15 GMT 2012
Rank295Aligned Residues86
% Identity15%Templated1xhca2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.35

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


   122.......130.........140.........150.........160.........170.........180.........190.... .....
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Query Sequence  SVPVWNGLTNEFHPTQLLADLLTMQEHLPGKAFNEMTLVYAGDARNNMGNSMLEAAALTGLDLRLVAPQACWP. . EAALV
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Template Sequence  REPQIKGK. EYLLTLRTIFDADRIKESIE. . . . NSGEAIIIG. . GGFIGLELAGNLAEAGYHVKLIHRGAMFLGLDEELS
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SBTG.GG


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STT

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TT

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   106...110... ......120.........130... ......140.. .......150.........160.........170........
 
   200.........210....
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Query Sequence  TECRALAQQNGGNIT
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Template Sequence  NMIKDMLEETGVKFF
Template Known Secondary structure  TT
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   179180.........190...
 
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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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