5FD0

Streptomyces plicatus N-acetyl-beta-hexosaminidase in complex with NAGlucal

Summary for 5FD0

Entry DOI	10.2210/pdb5fd0/pdb
Related	1HP4 1HP5 1JAK 1M01 5FCZ
Descriptor	B-N-acetylhexosaminidase, 2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (5 entities in total)
Functional Keywords	family 20 glycoside hydrolase, sphex, gh20, nag-glucal, hexosaminidase, glycosidase inhibitor, hydrolase
Biological source	Streptomyces plicatus
Total number of polymer chains	1
Total formula weight	56916.43
Authors	Vadlamani, G.,Mark, B.L. (deposition date: 2015-12-15, release date: 2016-10-26, Last modification date: 2023-09-27)
Primary citation	Santana, A.G.,Vadlamani, G.,Mark, B.L.,Withers, S.G. N-Acetyl glycals are tight-binding and environmentally insensitive inhibitors of hexosaminidases. Chem.Commun.(Camb.), 52:7943-7946, 2016 Cited by PubMed Abstract: Mono-, di- and trisaccharide derivatives of 1,2-unsaturated N-acetyl-d-glucal have been synthesized and shown to function as tight-binding inhibitors/slow substrates of representative hexosaminidases. Turnover is slow and not observed in the thioamide analogue, allowing determination of the 3-dimensional structure of the complex. Inhibition is insensitive to pH and to mutation of key catalytic residues, consistent with the uncharged character of the inhibitor. These properties could render this inhibitor class less prone to development of resistance. PubMed: 27253678 DOI: 10.1039/c6cc02520j PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation