The Open Protein Structure Annotation Network
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    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title Crystal structure of Bifunctional coenzyme A synthase (CoA synthase) (18044849) from MUS MUSCULUS at 1.70 A resolution. To be published
    Site JCSG
    PDB Id 2f6r Target Id 354593
    Molecular Characteristics
    Source Mus musculus
    Alias Ids TPS1336,18044849, 89730, 281909, 289346, 289372, 289643, 89656 Molecular Weight 29947.71 Da.
    Residues 269 Isoelectric Point 8.56
    Sequence mavnrfrlengkeelalyqiqllkdqshneneedkvssssfrqrilgnllqppnerpelpsglyvlglt gisgsgkssvaqrlknlgayiidsdhlghrayapggpayqpvveafgtdilhkdgtinrkvlgsrvfgn kkqmkiltdivwpviaklareemdvavakgktlcvidaamlleagwqsmvhevwtvvipeteavrrive rdglseaaaqsrlqsqmsgqqlveqsnvvlstlweshvtqsqvekawnllqkrlpkayqtrn
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.70 Rfree 0.211
    Matthews' coefficent 2.54 Rfactor 0.178
    Waters 199 Solvent Content 51.26

    Ligand Information


    Google Scholar output for 2f6r
    1. The JCSG MR pipeline: optimized alignments, multiple models and parallel searches
    R Schwarzenbacher, A Godzik - Section D: Biological , 2007 - scripts.iucr.org
    2. The structure of Staphylococcus aureus phosphopantetheine adenylyltransferase in complex with 3'-phosphoadenosine 5'-phosphosulfate reveals a new ligand-
    HH Lee, HJ Yoon, JY Kang, JH Park, DJ Kim - Section F: Structural , 2009 - scripts.iucr.org
    3. Crystal structure of phosphopantetheine adenylyltransferase from Enterococcus faecalis in the ligand-unbound state and in complex with ATP and pantetheine
    HJ Yoon, JY Kang, B Mikami, HH Lee, SW Suh - Molecules and cells, 2011 - Springer

    Protein Summary

    The gene 18044849 from Mus musculus encodes the enzyme dephospho-CoA kinase PF01121 EC2.7.1.24.  This enzyme belongs to the family of transferases.  The enzyme catalyzes the final step in CoA biosynthesis.  The protein belongs to the class of alpha and beta (a+b) proteins, and reveals  P-loop containing nucleoside triphosphate hydrolases fold type SCOP52539.  The protein consists of three domains: the nucleotide-binding domain with a five-stranded parallel beta-sheet, the substrate-binding alpha-helical domain, and the lid domain formed by a pair of alpha-helices.  The overall topology of the protein resembles the structures of other nucleotide kinases [Ref].  The structures of the enzyme homologues from other organisms have been solved: 1VHT, E.coli; 2IF2Aquifex aeolicus; 2GRJTHERMOTOGA MARITIMA.

    Ligand Summary





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