1EDT

CRYSTAL STRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H AT 1.9 ANGSTROMS RESOLUTION: ACTIVE SITE GEOMETRY AND SUBSTRATE RECOGNITION

Summary for 1EDT

• Entry DOI: 10.2210/pdb1edt/pdb
• Descriptor: ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H, ENDO H (2 entities in total)
• Functional Keywords: hydrolase (glucosidase)
• Biological source: Streptomyces plicatus
• Total number of polymer chains: 1
• Total formula weight: 29058.04

Authors

Van Roey, P.,Rao, V. (deposition date: 1995-03-31, release date: 1995-08-04, Last modification date: 2024-02-07)

Primary citation

Rao, V.,Guan, C.,Van Roey, P.
Crystal structure of endo-beta-N-acetylglucosaminidase H at 1.9 A resolution: active-site geometry and substrate recognition.
Structure, 3:449-457, 1995

PubMed Abstract: Endo-beta-N-acetylglucosaminidase H (Endo H), an endoglycosidase secreted by Streptomyces plicatus, hydrolyzes the glycosidic bond between the core N-acetyglucosamine residues of asparagine-linked high-mannose oligosaccharides. Endo H is a commonly used reagent in glycobiology research, including the characterization of oligosaccharides in glycoproteins. On-going crystallographic studies of Endo H and related endoglycosidases are aimed at identifying the molecular features that determine the different substrate specificities of these enzymes.

PubMed: 7663942
DOI: 10.1016/S0969-2126(01)00178-2

Experimental method

X-RAY DIFFRACTION (1.9 Å)