1SHO

CRYSTAL STRUCTURE OF VANCOMYCIN AT ATOMIC RESOLUTION

1SHO の概要

• エントリーDOI: 10.2210/pdb1sho/pdb
• 関連するPDBエントリー: 1AA5 1C0Q 1C0R 1FVM 1GAC 1GHG 1PN3 1PNV 1QD8 1RRV
• 関連するBIRD辞書のPRD_ID: PRD_000204
• 分子名称: VANCOMYCIN, vancosamine-(1-2)-beta-D-glucopyranose, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: glycopeptide, antibiotic
• 由来する生物種: AMYCOLATOPSIS ORIENTALIS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 3076.58

構造登録者

Sheldrick, G.M. (登録日: 1997-07-23, 公開日: 1997-12-24, 最終更新日: 2025-03-26)

主引用文献

Schafer, M.,Schneider, T.R.,Sheldrick, G.M.
Crystal Structure of Vancomycin.
Structure, 4:1509-, 1996

PubMed Abstract: Vancomycin and other related glycopeptide antibiotics are clinically very important because they often represent the last line of defence against bacteria that have developed resistance to antibiotics. Vancomycin is believed to act by binding nascent cell wall mucopeptides terminating in the sequence D-Ala-D-Ala, weakening the resulting cell wall. Extensive NMR and other studies have shown that the formation of asymmetric antibiotic dimers is important in peptide binding. Despite intensive efforts the crystal structure of vancomycin has been extremely difficult to obtain, partly because high-resolution data were unavailable, and partly because the structure was too large to be solved by conventional "direct methods'.

PubMed: 8994975
DOI: 10.1016/S0969-2126(96)00156-6

実験手法

X-RAY DIFFRACTION (1.09 Å)