Entry | Database: PDB / ID: 8cnc |
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Title | Structure of compound 1 bound KMT9 |
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Components | - Methyltransferase N6AMT1
- Multifunctional methyltransferase subunit TRM112-like protein
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Keywords | TRANSFERASE / protein methyltransferase / inhibitor / SAM analogue |
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Function / homology | Function and homology information
histone H4K12 methyltransferase activity / eRF1 methyltransferase complex / protein-glutamine N-methyltransferase activity / arsonoacetate metabolic process / : / peptidyl-glutamine methylation / rRNA (guanine-N7)-methylation / tRNA methyltransferase activator activity / toxin metabolic process / site-specific DNA-methyltransferase (adenine-specific) activity ...histone H4K12 methyltransferase activity / eRF1 methyltransferase complex / protein-glutamine N-methyltransferase activity / arsonoacetate metabolic process / : / peptidyl-glutamine methylation / rRNA (guanine-N7)-methylation / tRNA methyltransferase activator activity / toxin metabolic process / site-specific DNA-methyltransferase (adenine-specific) activity / tRNA modification in the nucleus and cytosol / Methylation / protein methyltransferase activity / positive regulation of rRNA processing / S-adenosylmethionine-dependent methyltransferase activity / tRNA methylation / S-adenosyl-L-methionine binding / rRNA methylation / rRNA modification in the nucleus and cytosol / negative regulation of gene expression, epigenetic / Eukaryotic Translation Termination / transcription initiation-coupled chromatin remodeling / Transferases; Transferring one-carbon groups; Methyltransferases / positive regulation of cell growth / methylation / nucleic acid binding / protein heterodimerization activity / perinuclear region of cytoplasm / protein-containing complex / nucleoplasm / nucleus / cytosolSimilarity search - Function Eukaryotic/archaeal PrmC-related / Multifunctional methyltransferase subunit Trm112 / Trm112-like / Trm112p-like protein / Methyltransferase small domain / Methyltransferase small domain / N-6 Adenine-specific DNA methylases signature. / DNA methylase, N-6 adenine-specific, conserved site / S-adenosyl-L-methionine-dependent methyltransferase superfamilySimilarity search - Domain/homology |
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Biological species | Homo sapiens (human) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.46 Å |
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Authors | Sheng, W. |
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Funding support | Germany, 6items Organization | Grant number | Country |
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German Research Foundation (DFG) | SFB850 | Germany | German Research Foundation (DFG) | SFB992 | Germany | German Research Foundation (DFG) | SFB1381 | Germany | German Research Foundation (DFG) | Schu688/15-1 | Germany | German Research Foundation (DFG) | FR01-374 | Germany | German Research Foundation (DFG) | EXC-2189 | Germany |
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Citation | Journal: To Be Published Title: Structure of compound 1 bound KMT9 Authors: Sheng, W. / Eric, M. / Roland, S. |
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History | Deposition | Feb 22, 2023 | Deposition site: PDBE / Processing site: PDBE |
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Revision 1.0 | Mar 6, 2024 | Provider: repository / Type: Initial release |
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