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The Open Protein Structure Annotation Network
PDB Keyword
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4lhs

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

    Title Crystal structure of a hypothetical protein (BACOVA_00914) from Bacteroides ovatus ATCC 8483 at 1.40 A resolution. To be published
    Site JCSG
    PDB Id 4lhs Target Id 416889
    Molecular Characteristics
    Source Bacteroides ovatus atcc 8483
    Alias Ids TPS72114,ZP_02063955.1, 334638 Molecular Weight 38341.08 Da.
    Residues 342 Isoelectric Point 8.88
    Sequence qqkdnityvpaqelllvgkattegeyfhrvdtakyrtmpptvkklftnsaglaisfttnspvikakwmv pdnyqlpnltrvaqkgldlyikrdgkwqfagvgipggvttekvlvdnmgteekecllylplydelksle igvssdahirkgenpfkekivvygssilqgasasrpgmayparlsrssgynfinlglsgngkmekevae mladidadafildcipnpspkeitdrtvdfvmtlrqkhpdtpiiviqtliretgnfnqkarenvkrqne aiaeqvevlrkknvknlyfikedqflgtdhegtvdgthpndlgfdrmlkkykpaiskilkikfkae
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.40 Rfree 0.1637
    Matthews' coefficent 2.07 Rfactor 0.1261
    Waters 376 Solvent Content 40.59

    Ligand Information
    Ligands
    Metals

    Jmol

     

    Protein Summary

    This is annotated as a protein of unknown function. FFAS shows significant hits, but < 20% sequence identity, to PDB ids 3skv (Ssfx3, highest sequence identity of 18% to this one), 2wab (endoglucanase E), 2w9x (putative acetate xylan esterase), 2waa (putative xylan esterase), 3dci (arylesterase), etc.

    Pfam update:  have built an N-term and a C-term family from this sequence. The N-term is strictly a DUF although I have called it GxDLY owing to a highly conserved sequence-motif. It is PF14607. The C-term matches SCOp superfamily:SGNH hydrolase [ 52266], but I have built a family, called Lipase_GDSL_3, PF14606.

    C-terminal domain (yellow-orange-red) appears to have the alpha/beta hydrolase fold found in GDSL hydrolases.

    This protein appears to be a carbohydrate hydrolase or a putative lipase.

    Fig1.png

    Ligand Summary

    Reviews

    References

     

    No references found.

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