3I53
Crystal structure of an O-methyltransferase (NcsB1) from neocarzinostatin biosynthesis in complex with S-adenosyl-L-homocysteine (SAH)
Summary for 3I53
Entry DOI | 10.2210/pdb3i53/pdb |
Related | 3I58 3I5U 3I64 |
Descriptor | O-methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, GLYCEROL, ... (4 entities in total) |
Functional Keywords | co-complex, rossmann-like fold, methyltransferase, transferase |
Biological source | Streptomyces carzinostaticus subsp. neocarzinostaticus |
Total number of polymer chains | 2 |
Total formula weight | 70127.13 |
Authors | Cooke, H.A.,Bruner, S.D. (deposition date: 2009-07-03, release date: 2009-09-01, Last modification date: 2023-09-06) |
Primary citation | Cooke, H.A.,Guenther, E.L.,Luo, Y.,Shen, B.,Bruner, S.D. Molecular basis of substrate promiscuity for the SAM-dependent O-methyltransferase NcsB1, involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin. Biochemistry, 48:9590-9598, 2009 Cited by PubMed: 19702337DOI: 10.1021/bi901257q PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.08 Å) |
Structure validation
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