Entry | Database: PDB / ID: 5yo2 |
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Title | The crystal structure of Rv2747 from Mycobacterium tuberculosis in complex with Acetyl CoA and L-Arginine |
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Components | Amino-acid acetyltransferase |
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Keywords | TRANSFERASE / Acetyltransferase |
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Function / homology | Function and homology information
methione N-acyltransferase activity / amino-acid N-acetyltransferase / acetyl-CoA:L-glutamate N-acetyltransferase activity / arginine biosynthetic process via ornithine / N-acetyltransferase activity / protein homotetramerization / protein homodimerization activity / cytoplasmSimilarity search - Function Amino-acid N-acetyltransferase / Acetyltransferase (GNAT) family / Gcn5-related N-acetyltransferase (GNAT) domain profile. / GNAT domain / Acyl-CoA N-acyltransferaseSimilarity search - Domain/homology |
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Biological species | Mycobacterium tuberculosis H37Rv (bacteria) |
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Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.997 Å |
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Authors | Singh, E. / Tiruttani Subhramanyam, U.K. / Pal, R.K. / Srinivasan, A. / Gourinath, S. / Das, U. |
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Citation | Journal: Int. J. Biol. Macromol. / Year: 2019 Title: Structural insights into the substrate binding mechanism of novel ArgA from Mycobacterium tuberculosis Authors: Das, U. / Singh, E. / Dharavath, S. / Tiruttani Subhramanyam, U.K. / Pal, R.K. / Vijayan, R. / Menon, S. / Kumar, S. / Gourinath, S. / Srinivasan, A. |
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History | Deposition | Oct 26, 2017 | Deposition site: PDBJ / Processing site: PDBJ |
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Revision 1.0 | Nov 7, 2018 | Provider: repository / Type: Initial release |
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