4YMH
Crystal structure of SAH-bound Podospora anserina methyltransferase PaMTH1
Summary for 4YMH
Entry DOI | 10.2210/pdb4ymh/pdb |
Related | 4QVK |
Descriptor | Putative SAM-dependent O-methyltranferase, S-ADENOSYL-L-HOMOCYSTEINE, DI(HYDROXYETHYL)ETHER, ... (4 entities in total) |
Functional Keywords | transferase, methylation |
Biological source | Podospora anserina |
Total number of polymer chains | 4 |
Total formula weight | 109712.61 |
Authors | Kudlinzki, D.,Linhard, V.L.,Chatterjee, D.,Saxena, K.,Sreeramulu, S.,Schwalbe, H. (deposition date: 2015-03-06, release date: 2015-05-27, Last modification date: 2024-01-10) |
Primary citation | Chatterjee, D.,Kudlinzki, D.,Linhard, V.,Saxena, K.,Schieborr, U.,Gande, S.L.,Wurm, J.P.,Wohnert, J.,Abele, R.,Rogov, V.V.,Dotsch, V.,Osiewacz, H.D.,Sreeramulu, S.,Schwalbe, H. Structure and Biophysical Characterization of the S-Adenosylmethionine-dependent O-Methyltransferase PaMTH1, a Putative Enzyme Accumulating during Senescence of Podospora anserina. J.Biol.Chem., 290:16415-16430, 2015 Cited by PubMed: 25979334DOI: 10.1074/jbc.M115.660829 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.876 Å) |
Structure validation
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