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TitleComputational Design of Experiment Unveils the Conformational Reaction Coordinate of GH125 alpha-Mannosidases.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 139, Page 1085-1088, Year 2017
Publish dateOct 27, 2016 (structure data deposition date)
AuthorsAlonso-Gil, S. / Males, A. / Fernandes, P.Z. / Williams, S.J. / Davies, G.J. / Rovira, C.
External linksJ. Am. Chem. Soc. / PubMed:28026180
MethodsX-ray diffraction
Resolution1.55 - 2.1 Å
Structure data

PDB-5m7i:
Crystal structure of GH125 1,6-alpha-mannosidase mutant from Clostridium perfringens in complex with 1,6-alpha-mannobiose
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-5m7y:
Crystal structure of GH125 1,6-alpha-mannosidase mutant from Clostridium perfringens in complex with 1,6-alpha-mannotriose
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

Source
  • clostridium perfringens (strain 13 / type a) (bacteria)
KeywordsHYDROLASE / Mannosidase / Carbohydrate chemistry / Glycoside Hydrolase / Carbohydrate

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