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Structure of radical S-adenosylmethionine methyltransferase, NocN, from Nocardia with SAH and side-ring closed product analog bound

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Protein Data Bank Japan2026-08-12 更新2026-08-24 收录
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Structure of radical S-adenosylmethionine methyltransferase, NocN, from Nocardia with SAH and side-ring closed product analog bound Descriptor: 2-[(6S,13S)-6-[(2-{(1S,2R)-1-[(N-{2-[(1S)-1-amino-2-hydroxyethyl]-1,3-thiazole-4-carbonyl}-L-threonyl)amino]-2-hydroxypropyl}-1,3-thiazole-4-carbonyl)amino]-18-methyl-3,11,16-trioxo-1,3,4,5,6,11,12,13,14,16-decahydro-10,7-(azeno)-17,19-epimino-2,15,8,12-benzodioxathiazacycloicosin-13-yl]-1,3-thiazole-4-carboxylic acid, CALCIUM ION, IRON/SULFUR CLUSTER, ... Authors: Wang, B, Knox, H.L, York, N.J, Radle, M.I, Silakov, A, Booker, S.J. Deposit date: 2025-06-13 Release date: 2026-06-03 Last modified: 2026-08-12 Method: X-RAY DIFFRACTION (1.78 Å) Cite: Structural and Spectroscopic Basis for Catalysis by a Class C Radical S -Adenosylmethionine Methylase Involved in Nosiheptide/Nocathiacin Biosynthesis. J.Am.Chem.Soc., 148, 2026

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2025-06-13
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