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TitleAn atypical interaction explains the high-affinity of a non-hydrolyzable S-linked 1,6-alpha-mannanase inhibitor.
Journal, issue, pagesChem. Commun. (Camb. ), Vol. 53, Page 9238-9241, Year 2017
Publish dateOct 26, 2016 (structure data deposition date)
AuthorsBelz, T. / Jin, Y. / Coines, J. / Rovira, C. / Davies, G.J. / Williams, S.J.
External linksChem. Commun. (Camb. ) / PubMed:28766587
MethodsX-ray diffraction
Resolution1.46 - 1.69 Å
Structure data

PDB-5m77:
a GH76 family enzyme structure
Method: X-RAY DIFFRACTION / Resolution: 1.46 Å

PDB-5n0f:
The catalytic domain, BcGH76, of Bacillus circulans Aman6 in complex with 1,6-ManSIFG
Method: X-RAY DIFFRACTION / Resolution: 1.69 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-7K2:
[(3S,4R,5R)-4,5-dihydroxypiperidin-3-yl]methyl 1-thio-alpha-D-mannopyranoside

Source
  • bacillus circulans (bacteria)
KeywordsHYDROLASE / glycoside HYDROLASE / complex / mannanase / S-linked polysaccharide

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