1SHO

CRYSTAL STRUCTURE OF VANCOMYCIN AT ATOMIC RESOLUTION

Summary for 1SHO

• Entry DOI: 10.2210/pdb1sho/pdb
• Related: 1AA5 1C0Q 1C0R 1FVM 1GAC 1GHG 1PN3 1PNV 1QD8 1RRV
• Related PRD ID: PRD_000204
• Descriptor: VANCOMYCIN, vancosamine-(1-2)-beta-D-glucopyranose, ACETATE ION, ... (5 entities in total)
• Functional Keywords: glycopeptide, antibiotic
• Biological source: AMYCOLATOPSIS ORIENTALIS
• Total number of polymer chains: 2
• Total formula weight: 3076.58

Authors

Sheldrick, G.M. (deposition date: 1997-07-23, release date: 1997-12-24, Last modification date: 2020-07-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.09 Å)