5N0F

The catalytic domain, BcGH76, of Bacillus circulans Aman6 in complex with 1,6-ManSIFG

Summary for 5N0F

Entry DOI	10.2210/pdb5n0f/pdb
Descriptor	Alpha-1,6-mannanase, [(3S,4R,5R)-4,5-dihydroxypiperidin-3-yl]methyl 1-thio-alpha-D-mannopyranoside (3 entities in total)
Functional Keywords	glycoside hydrolase, complex, mannanase, s-linked polysaccharide, hydrolase
Biological source	Bacillus circulans
Total number of polymer chains	2
Total formula weight	82512.48
Authors	Jin, Y.,Williams, S.,Davies, G. (deposition date: 2017-02-02, release date: 2017-08-09, Last modification date: 2024-01-17)
Primary citation	Belz, T.,Jin, Y.,Coines, J.,Rovira, C.,Davies, G.J.,Williams, S.J. An atypical interaction explains the high-affinity of a non-hydrolyzable S-linked 1,6-alpha-mannanase inhibitor. Chem. Commun. (Camb.), 53:9238-9241, 2017 Cited by PubMed Abstract: The non-hydrolyzable S-linked azasugars, 1,6-α-mannosylthio- and 1,6-α-mannobiosylthioisofagomine, were synthesized and shown to bind with high affinity to a family 76 endo-1,6-α-mannanase from Bacillus circulans. X-ray crystallography showed an atypical interaction of the isofagomine nitrogen with the catalytic acid/base. Molecular dynamics simulations reveal that the atypical binding results from sulfur perturbing the most stable form away from the nucleophile interaction preferred for the O-linked congener. PubMed: 28766587 DOI: 10.1039/c7cc04977c PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.69 Å)

Structure validation