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Job DescriptionP0AG84
Confidence99.45%DateWed Jan 25 15:20:34 GMT 2012
Rank210Aligned Residues186
% Identity21%Templatec2fr1A_
PDB info PDB header:oxidoreductaseChain: A: PDB Molecule:erythromycin synthase, eryai; PDBTitle: the first ketoreductase of the erythromycin synthase2 (crystal form 2)
Resolution1.79 Å

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


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Query Sequence  EKTYVGSGRLKDRKALVTGGDSGIGRAAAIAYAREGA. DVAISYLP. VEEEDAQDVKKIIEECGRKAVLLPGDLSDEKFA
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Template Sequence  AAPATDDEWKPTGTVLVTGGTGGVGGQIARWLARRGAPHLLLVSRSGPDADGAGELVAELEALGARTTVAACDVTDRESV
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   1654.....1660.........1670.........1680.........1690.........1700.........1710.........1720.........1730...
 
   116...120.........130.........140.........150.........160.........170.........180.........190.....
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Query Sequence  RSLVHEAHKALGGLDIMALVAGKQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPKGASIITTSSIQAYQPSPH
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Template Sequence  RELLGGIGDDV. PLSAVFHAAATLDDGT. VDTLTGERIERASRAKVLGARNLHELTREL. . DLTAFVLFSSFASAFGAPG
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   1734.....1740.... .....1750.........1760 .........1770.........1780.........1790 .........1800.........
 
   196...200.........210.........220.........230.
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Query Sequence  LLDYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGP
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Template Sequence  LGGYAPGNAYLDGLAQQRRSD. . . . GLPATAVAWGT
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   1810.........1820.........1830 .........1840.
 
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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