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The Open Protein Structure Annotation Network
PDB Keyword
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2kl2

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

    Title Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites. Acta Crystallogr.,Sect.F 66 1393-1405 2010
    Site JCSG
    PDB Id 2kl2 Target Id 354528
    Related PDB Ids 1vkb 
    Molecular Characteristics
    Source Mus musculus
    Alias Ids TPS1333,13879369, 89629, 89786, 89841, 289322, 289411, 289508 Molecular Weight 17079.35 Da.
    Residues 149 Isoelectric Point 5.10
    Sequence mahifvygtlkrgqpnhkvmldhshglaafrgrgctvesfplviagehnipwllylpgkghcvtgeiye vdeqmlrflddfedcpsmyqrtalqvqvlewegdgdpgdsvqcfvyttatyapewlflpyhesydsegp hglrynprenr
      BLAST   FFAS

    Structure Determination
    Method NMR Chains 1

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 2kl2
    1. Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites
    P Serrano, B Pedrini, M Geralt, K Jaudzems - Section F: Structural , 2010 - scripts.iucr.org
     
    2. The J-UNIO protocol for automated protein structure determination by NMR in solution
    P Serrano, B Pedrini, B Mohanty, M Geralt - Journal of biomolecular , 2012 - Springer
     

    Protein Summary

    Gene a2ld1 from Mus musculus encodes the NP_663441 amino acid sequence that belongs to the AIG2-like group (PF06094). It has some similarity to uncharacterized proteins involved in cation transport (COG3703).

    SCOP classifies 2kl2 structure in the alpha+beta class, gamma-glutamyl cyclotransferase (GGCT)-like (super)family. Significant structural similarity to GGCT like PDB:3jub (Z-scr=21), PDB:2qik (Z-scr=12), PDB:1v30 (Z-scr=10), and PDB:2g0q, PDB:2i5t, PDB:1xhs (Z-scr=9) is detected by DALI.

    Analysis of the crystallographic packing of 1vkb (crystal structure of 2kl2) using the PQS server {Henrick, 1998 #73} indicates that a monomer is the biologically relevant form. Conserved residues (Pro51, Tyr88, Phe113, Tyr115) form a long cleft. Two formic acid  molecules (from the crystallization solution) are present in this cleft. Conserved Asp79 is not part of the cleft but interacts with Tyr115. The second (separate) cluster of conserved residues includes Glu65, Tyr68, and His117 [Ref].

    Ligand Summary



    References

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