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The Open Protein Structure Annotation Network
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2ord

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

    Title Crystal structure of Acetylornithine aminotransferase (EC 2.6.1.11) (ACOAT) (TM1785) from Thermotoga maritima at 1.40 A resolution. To be published
    Site JCSG
    PDB Id 2ord Target Id 283638
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1316,TM1785, 3.40.640.10, 289554 Molecular Weight 42882.08 Da.
    Residues 385 Isoelectric Point 6.00
    Sequence mylmntysrfpatfvygkgswiydekgnayldftsgiavnvlghshprlveaikdqaeklihcsnlfwn rpqmelaellskntfggkvffantgteaneaaikiarkygkkksekkyrilsahnsfhgrtlgsltatg qpkyqkpfeplvpgfeyfefnnvedlrrkmsedvcavflepiqgesgivpatkefleearklcdeydal lvfdevqcgmgrtgklfayqkygvvpdvlttakglgggvpigavivneranvlepgdhgttfggnplac ragvtvikeltkegfleeveekgnylmkklqemkeeydvvadvrgmglmigiqfreevsnrevatkcfe nkllvvpagnntirflppltveygeidlavetlkkvlqgi
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 1.40 Rfree 0.17
    Matthews' coefficent 2.33 Rfactor 0.148
    Waters 675 Solvent Content 47.15

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 2ord
    1. Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard
    TC Terwilliger, PD Adams, RJ Read - Section D: Biological , 2009 - scripts.iucr.org
     
    2. PURIFICATION OF LYSINE DECARBOXYLASE: A MODEL SYSTEM FOR PLP ENZYME INHIBITOR DEVELOPMENT AND STUDY
    LC Zohner - 2011 - digitalcommons.unl.edu
     

    Protein Summary

    TM1785 is involved in arginine biosynthesis pathway. This structure is highly similar to other homologous structures already deposited in pdb. The structure may be can be studied together with other Arg biosynthesis proteins such as TM1783.

    1vef/1wkg/1wkh (seq id 43%)
    1lx9 (seq id 39%) 1z7d (36%)
    2byj /1oat/2oat/1gbn(35%)

    Ligand Summary



    References

    Reviews

    References

     

    No references found.

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