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Job DescriptionP37596
Confidence98.86%DateThu Jan 5 11:55:42 GMT 2012
Rank227Aligned Residues115
% Identity23%Templated1gesa2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution1.74

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


   121........130.........140.........150.........160.........170.........180.........190.........200
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Query Sequence  LMLTLNSQQEYRACETQLRDARRVLIVGGGLIGSELAMDFCRAGKAVTLIDNAASILASLMPPEVSSRLQHRLTEMGVHL
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Template Sequence  DIPGVEYGIDSDGFFALPALPERVAVVGAGYIGVELGGVINGLGAKTHLFEMFDAPLP. SFDPMISETLVEVMNAEGPQL
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TTGGGSB

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   147..150.........160.........170.........180.........190.........200.... .....210.........220.....
 
   201........210...... ...220.........230......
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Query Sequence  LLKSQLQGLEKTDSGI. QATLDRQRNIEVDAVIAATG
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Template Sequence  HTNAIPKAVVKNTDGSLTLELEDGRSETVDCLIWAIG
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   226...230.........240.........250.........260..
 
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]
 
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Lawrence Kelley, Benjamin Jefferys 
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