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Job DescriptionP75905
Confidence54.14%DateThu Jan 5 12:15:52 GMT 2012
Rank78Aligned Residues103
% Identity18%Templatec2v0hA_
PDB info PDB header:transferaseChain: A: PDB Molecule:bifunctional protein glmu; PDBTitle: characterization of substrate binding and catalysis of the2 potential antibacterial target n-acetylglucosamine-1-3 phosphate uridyltransferase (glmu)
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  IIPCFNEEKNVEETIHAALAQRYENIEVIAVNDGSTDKTRAILDRMAAQIPHLRVIHLAQNQGKAIALKTGAAAAKS. EY
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Template Sequence  LHTIAGKP. MVKHVIDTAHQLGS. . ENIHLIYGHGGDLMRTHL. . . . . ANEQVNWVLQTEQLGTAHAVQQAAPFFKDNEN
Template Known Secondary structure  GSTT.TT
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Query Sequence  LVCIDGDA. LLDRDAAAYIVEPMLYNPRVGAVT
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Template Sequence  IVVLYGDAPLITKETLEKLIEAKPENGIALLTV
Template Known Secondary structure  TT
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   99100.........110.........120.........130.
 
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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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