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Job DescriptionP09832
Confidence98.40%DateThu Jan 5 11:02:29 GMT 2012
Rank272Aligned Residues85
% Identity25%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


   146...150.........160.........170.........180.........190.........200.........210......... 220.
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Query Sequence  GKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEV. . . . GR
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Template Sequence  SGEAIIIGGGFIGLELAGNLAEAGYHVKLIHRGAMFLG. . . . . . . . . . LDEELSNMIKDMLEETGVKFFLNSELLEANEE
Template Known Secondary structure  S
STT

SSS

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TT
S


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   135....140.........150.........160.........170.. .......180.........190.........200....
 
   222.......230.........240
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Query Sequence  DVQLDDLLSDYDAVFLGVG
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Template Sequence  GVLTNSGFIEGKVKICAIG
Template Known Secondary structure  TT
S


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   205....210.........220...
 
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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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