Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	N-Substituted Valiolamine Derivatives as Potent Inhibitors of Endoplasmic Reticulum alpha-Glucosidases I and II with Antiviral Activity.
Journal, issue, pages	J. Med. Chem., Vol. 64, Page 18010-18024, Year 2021
Publish date	Aug 18, 2020 (structure data deposition date)
Authors	Karade, S.S. / Hill, M.L. / Kiappes, J.L. / Manne, R. / Aakula, B. / Zitzmann, N. / Warfield, K.L. / Treston, A.M. / Mariuzza, R.A.
External links	J. Med. Chem. / PubMed:34870992
Methods	X-ray diffraction
Resolution	2.07 - 2.55 Å
Structure data	PDB-7jty: Co-crystal structure of alpha glucosidase with compound 1 Method: X-RAY DIFFRACTION / Resolution: 2.21 Å PDB-7k9n: Co-crystal structure of alpha glucosidase with compound 2 Method: X-RAY DIFFRACTION / Resolution: 2.07 Å PDB-7k9o: Co-crystal structure of alpha glucosidase with compound 3 Method: X-RAY DIFFRACTION / Resolution: 2.302 Å PDB-7k9q: Co-crystal structure of alpha glucosidase with compound 4 Method: X-RAY DIFFRACTION / Resolution: 2.3 Å PDB-7k9t: Co-crystal structure of alpha glucosidase with compound 5 Method: X-RAY DIFFRACTION / Resolution: 2.1 Å PDB-7kad: Co-crystal structure of alpha glucosidase with compound 6 Method: X-RAY DIFFRACTION / Resolution: 2.506 Å PDB-7kb6: Co-crystal structure of alpha glucosidase with compound 7 Method: X-RAY DIFFRACTION / Resolution: 2.2 Å PDB-7kb8: Co-crystal structure of alpha glucosidase with compound 8 Method: X-RAY DIFFRACTION / Resolution: 2.385 Å PDB-7kbj: Co-crystal structure of alpha glucosidase with compound 9 Method: X-RAY DIFFRACTION / Resolution: 2.21 Å PDB-7kbr: Co-crystal structure of alpha glucosidase with compound 10 Method: X-RAY DIFFRACTION / Resolution: 2.09 Å PDB-7kry: Co-crystal structure of alpha glucosidase with compound 11 Method: X-RAY DIFFRACTION / Resolution: 2.55 Å PDB-7l9e: Crystal structure of apo-alpha glucosidase Method: X-RAY DIFFRACTION / Resolution: 2.29 Å
Chemicals	ChemComp-VND: (1S,2S,3R,4S,5S)-5-(butylamino)-1-(hydroxymethyl)cyclohexane-1,2,3,4-tetrol ChemComp-SO4: SULFATE ION ChemComp-EDO: 1,2-ETHANEDIOL ChemComp-PEG: DI(HYDROXYETHYL)ETHER ChemComp-CA: Unknown entry ChemComp-HOH: WATER ChemComp-W9G: (1S,2S,3R,4S,5S)-1-(hydroxymethyl)-5-[(9-methoxynonyl)amino]cyclohexane-1,2,3,4-tetrol ChemComp-PGE: TRIETHYLENE GLYCOL ChemComp-PG4: TETRAETHYLENE GLYCOL / precipitantYM ChemComp-W9P: (1~{S},2~{S},3~{R},4~{S},5~{S})-1-(hydroxymethyl)-5-[6-[[2-[oxidanyl(oxidanylidene)-$l^{4}-azanyl]-4-(1,2,3,4-tetrazol-1-yl)phenyl]amino]hexylamino]cyclohexane-1,2,3,4-tetrol ChemComp-W9S: (1S,2S,3R,4S,5S)-5-amino-1-(hydroxymethyl)cyclohexane-1,2,3,4-tetrol ChemComp-W9V: (1S,2S,3R,4S,5S)-1-(hydroxymethyl)-5-{[(5Z)-6-{[2-nitro-4-(2H-1,2,3-triazol-2-yl)phenyl]amino}hex-5-en-1-yl]amino}cyclohexane-1,2,3,4-tetrol ChemComp-P6G: HEXAETHYLENE GLYCOL / precipitantYM ChemComp-W9Y: (1S,2S,3R,4S,5S)-1-(hydroxymethyl)-5-[(6-{[2-nitro-4-(1H-1,2,3-triazol-1-yl)phenyl]amino}hexyl)amino]cyclohexane-1,2,3,4-tetrol ChemComp-XOD: (1S,2S,3R,4S,5S)-1-(hydroxymethyl)-5-[(6-{[2-nitro-4-(pyrimidin-2-yl)phenyl]amino}hexyl)amino]cyclohexane-1,2,3,4-tetrol ChemComp-WA7: (1S,2S,3R,4S,5S)-1-(hydroxymethyl)-5-[(4-{[2-nitro-4-(triazan-1-yl)phenyl]amino}butyl)amino]cyclohexane-1,2,3,4-tetrol ChemComp-WAV: (1S,2S,3R,4S,5S)-1-(hydroxymethyl)-5-{[2-(2-{[2-nitro-4-(triazan-1-yl)phenyl]amino}ethoxy)ethyl]amino}cyclohexane-1,2,3,4-tetrol ChemComp-WAS: 2-{[2-nitro-4-(triazan-1-yl)phenyl]amino}ethyl (2-{[(1S,2S,3R,4S,5S)-2,3,4,5-tetrahydroxy-5-(hydroxymethyl)cyclohexyl]amino}ethyl)carbamate ChemComp-X8Y: (1S,2S,3R,4S,5S)-5-({6-[(4-azido-2-nitrophenyl)amino]hexyl}amino)-1-(hydroxymethyl)cyclohexane-1,2,3,4-tetrol
Source	mus musculus (house mouse)
Keywords	HYDROLASE / Alpha Glucosidase II / Endoplasmic reticulum / Inhibitor complex / HYDROLASE-INHIBITOR complex / Hydrolases