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Job DescriptionP77650
Confidence99.00%DateThu Jan 5 12:31:22 GMT 2012
Rank242Aligned Residues114
% Identity15%Templated1onfa2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.60

  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.........200.
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Query Sequence  GERCFTLRHAGDAARLREVLQPERSVVIIGAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGV
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Template Sequence  FPPVKGIENTISSDEFFNIKE. SKKIGIVGSGYIAVELINVIKRLGIDSYIFARGNRIL. RKFDESVINVLENDMKKNNI
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   154.....160.........170.... .....180.........190.........200.........210. ........220.........230.
 
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Query Sequence  RILLNNAIEHVV. . DGEKVELTLQSGETL. QADVVIYGI
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Template Sequence  NIVTFADVVEIKKVSDKNLSIHLSDGRIYEHFDHVIYCV
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   232.......240.........250.........260.........270
 
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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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