4YMG

Crystal structure of SAM-bound Podospora anserina methyltransferase PaMTH1

Summary for 4YMG

• Entry DOI: 10.2210/pdb4ymg/pdb
• Related: 4QVK
• Descriptor: Putative SAM-dependent O-methyltranferase, S-ADENOSYLMETHIONINE, PHOSPHATE ION, ... (6 entities in total)
• Functional Keywords: transferase, methylation
• Biological source: Podospora anserina
• Total number of polymer chains: 2
• Total formula weight: 55175.56

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; PubMed: 25979334; DOI: 10.1074/jbc.M115.660829

Experimental method

X-RAY DIFFRACTION (1.899 Å)