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    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary

    Title Crystal structure of a HD-domain phosphohydrolase (lin2634) from LISTERIA INNOCUA at 1.98 A resolution. To be published
    Site JCSG
    PDB Id 3mzo Target Id 394139
    Molecular Characteristics
    Source Listeria innocua clip11262
    Alias Ids TPS25775,NP_471964.1, _0077.001156_ Molecular Weight 24846.84 Da.
    Residues 215 Isoelectric Point 4.88
    Sequence mgihqyfqslsdleniyrcpgkfkyqehsvaehsykvtsiaqffgaveedagnevnwralyekalnhdy selfigdiktpvkyattelremlseveesmtknfisreipatfqpiyrhllkegkdstlegkilaisdk vdllyesfgeiqkgnpenifveiysealatiyeyremasvkyflkeilpdmlaekgiektelpqlttei ttkalrde
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.98 Rfree 0.200
    Matthews' coefficent 2.32 Rfactor 0.166
    Waters 378 Solvent Content 47.07

    Ligand Information



    Protein Summary

    Lin2634 (Fig.1) from is likely a  HD-domain phosphohydrolase (PFAM PF01966), it has 24% seq id with  YfbR from Escherichia coli [Ref], which is a 5'-deoxyribonucleotidase (pdb 2paq). The two structures can be superimposed with a rmsd of 2.3A for 170 aligned Ca. The active site (Arg18, His33, Asp137, His67 etc) is also very similar. However, the residues at the perimeter is not conserved, suggesting possible difference in substrate specificity. It is likely Lin2634 functions as a hexamer (Fig 2).


    Two calcium ions from crystallization conditions are present in the putative metal binding sites (Fig 1).


    Fig. 1. Structure of Lin2634


    Fig. 2. Hexamer of Lin2634 (2 views, rotate around x by 90)


    Ligand Summary




    1. (No Results)


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    Files (3)

    FileSizeDateAttached by 
    MH11582F hexamer view 1
    219.51 kB19:49, 15 Apr 2010qxuActions
    MH11582F hexamer view 2
    219.78 kB19:49, 15 Apr 2010qxuActions
    MH11582F monomer
    139.49 kB19:49, 15 Apr 2010qxuActions
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