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Job DescriptionP09832
Confidence98.63%DateThu Jan 5 11:02:29 GMT 2012
Rank249Aligned Residues90
% Identity22%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


   142.......150.........160.........170.........180.........190.........200.........210.........220.
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Query Sequence  VKQTGKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEVGR
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Template Sequence  LPALPERVAVVGAGYIGVELGGVINGLGAKTHLFEMFDAPL. . . . . . . . . PSFDPMISETLVEVMNAEGPQLHTNAIPKA
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   163......170.........180.........190.........200... ......210.........220.........230...
 
   222.......230 .........240
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Query Sequence  DVQLDDLLS. . . . . . . . . . DYDAVFLGVG
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Template Sequence  VVKNTDGSLTLELEDGRSETVDCLIWAIG
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   234.....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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