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Job DescriptionP0A9P0
Confidence98.67%DateThu Jan 5 11:10:52 GMT 2012
Rank280Aligned Residues111
% Identity33%Templated1lvla2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.45

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


   158.160.........170.........180.........190.........200.........210.........220.... .....230......
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Query Sequence  EDPRIWDSTDALELKEVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDIVKVFTK. RISKKFNLMLET
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Template Sequence  LGGPVISSTEALAPKALPQHLVVVGGGYIGLELGIAYRKLGAQVSVVEARERILPTYDSELTAPVAESLKKLGIALHLGH
Template Known Secondary structure 
BTT
T

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S

ST

SSSSSSTTS
T
TT
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   154.....160.........170.........180.........190.........200.........210.........220.........230...
 
   237..240.........250.........260.........270..
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Query Sequence  KVTAVEAKEDGIYVTMEGKKAPAEPQRYDAVLVAIG
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Template Sequence  SVEGYENG. . . . CLLANDGKGGQLRLEADRVLVAVG
Template Known Secondary structure  TT....
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   234.....240. ........250.........260.....
 
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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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