4L4Q
Methionine Adenosyltransferase
Summary for 4L4Q
| Entry DOI | 10.2210/pdb4l4q/pdb |
| Descriptor | S-adenosylmethionine synthase (2 entities in total) |
| Functional Keywords | transferase, cytoplasmic |
| Biological source | Thermococcus kodakarensis |
| Total number of polymer chains | 4 |
| Total formula weight | 178691.64 |
| Authors | Schlesier, J.,Siegrist, J.,Gerhardt, S.,Andexer, J.N.,Einsle, O. (deposition date: 2013-06-09, release date: 2014-03-19, Last modification date: 2024-02-28) |
| Primary citation | Schlesier, J.,Siegrist, J.,Gerhardt, S.,Erb, A.,Blaesi, S.,Richter, M.,Einsle, O.,Andexer, J.N. Structural and functional characterisation of the methionine adenosyltransferase from Thermococcus kodakarensis. Bmc Struct.Biol., 13:22-22, 2013 Cited by PubMed Abstract: Methionine adenosyltransferases catalyse the synthesis of S-adenosylmethionine, a cofactor abundant in all domains of life. In contrast to the enzymes from bacteria and eukarya that show high sequence similarity, methionine adenosyltransferases from archaea diverge on the amino acid sequence level and only few conserved residues are retained. PubMed: 24134203DOI: 10.1186/1472-6807-13-22 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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