1MYR
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![BU of 1myr by Molmil](/molmil-images/mine/1myr) | MYROSINASE FROM SINAPIS ALBA | Descriptor: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCEROL, ... | Authors: | Burmeister, W.P, Iori, R, Palmieri, S, Henrissat, B. | Deposit date: | 1997-03-23 | Release date: | 1997-06-16 | Last modified: | 2023-08-09 | Method: | X-RAY DIFFRACTION (1.64 Å) | Cite: | The crystal structures of Sinapis alba myrosinase and a covalent glycosyl-enzyme intermediate provide insights into the substrate recognition and active-site machinery of an S-glycosidase. Structure, 5, 1997
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1DWH
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![BU of 1dwh by Molmil](/molmil-images/mine/1dwh) | |
1DWF
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![BU of 1dwf by Molmil](/molmil-images/mine/1dwf) | |
1DWI
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![BU of 1dwi by Molmil](/molmil-images/mine/1dwi) | |
1E4M
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![BU of 1e4m by Molmil](/molmil-images/mine/1e4m) | MYROSINASE FROM SINAPIS ALBA | Descriptor: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCEROL, ... | Authors: | Burmeister, W.P. | Deposit date: | 2000-07-10 | Release date: | 2001-05-25 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.2 Å) | Cite: | High Resolution X-Ray Crystallography Shows that Ascorbate is a Cofactor for Myrosinase and Substitutes for the Function of the Catalytic Base J.Biol.Chem., 275, 2000
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1DWG
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![BU of 1dwg by Molmil](/molmil-images/mine/1dwg) | |
1DWA
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![BU of 1dwa by Molmil](/molmil-images/mine/1dwa) | |
1DWJ
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![BU of 1dwj by Molmil](/molmil-images/mine/1dwj) | |
1E6S
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![BU of 1e6s by Molmil](/molmil-images/mine/1e6s) | MYROSINASE FROM SINAPIS ALBA with bound gluco-hydroximolactam and sulfate | Descriptor: | (2S,3S,4R,5R)-6-(HYDROXYAMINO)-2-(HYDROXYMETHYL)-2,3,4,5-TETRAHYDROPYRIDINE-3,4,5-TRIOL, 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... | Authors: | Burmeister, W.P. | Deposit date: | 2000-08-23 | Release date: | 2000-09-06 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.35 Å) | Cite: | High Resolution X-Ray Crystallography Shows that Ascorbate is a Cofactor for Myrosinase and Substitutes for the Function of the Catalytic Base J.Biol.Chem., 275, 2000
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1E70
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![BU of 1e70 by Molmil](/molmil-images/mine/1e70) | 2-F-glucosylated MYROSINASE FROM SINAPIS ALBA | Descriptor: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-deoxy-2-fluoro-alpha-D-glucopyranose, ... | Authors: | Burmeister, W.P. | Deposit date: | 2000-08-23 | Release date: | 2001-01-05 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.65 Å) | Cite: | High Resolution X-Ray Crystallography Shows that Ascorbate is a Cofactor for Myrosinase and Substitutes for the Function of the Catalytic Base J.Biol.Chem., 275, 2000
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1E72
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![BU of 1e72 by Molmil](/molmil-images/mine/1e72) | Myrosinase from Sinapis alba with bound gluco-hydroximolactam and sulfate or ascorbate | Descriptor: | (2S,3S,4R,5R)-6-(HYDROXYAMINO)-2-(HYDROXYMETHYL)-2,3,4,5-TETRAHYDROPYRIDINE-3,4,5-TRIOL, 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... | Authors: | Burmeister, W.P. | Deposit date: | 2000-08-23 | Release date: | 2001-01-05 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.6 Å) | Cite: | High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base. J. Biol. Chem., 275, 2000
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1E6Q
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![BU of 1e6q by Molmil](/molmil-images/mine/1e6q) | MYROSINASE FROM SINAPIS ALBA with the bound transition state analogue gluco-tetrazole | Descriptor: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCEROL, ... | Authors: | Burmeister, W.P. | Deposit date: | 2000-08-22 | Release date: | 2001-01-05 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.35 Å) | Cite: | High Resolution X-Ray Crystallography Shows that Ascorbate is a Cofactor for Myrosinase and Substitutes for the Function of the Catalytic Base J.Biol.Chem., 275, 2000
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1E71
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![BU of 1e71 by Molmil](/molmil-images/mine/1e71) | MYROSINASE FROM SINAPIS ALBA with bound ascorbate | Descriptor: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ASCORBIC ACID, ... | Authors: | Burmeister, W.P. | Deposit date: | 2000-08-23 | Release date: | 2001-01-05 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.5 Å) | Cite: | High Resolution X-Ray Crystallography Shows that Ascorbate is a Cofactor for Myrosinase and Substitutes for the Function of the Catalytic Base J.Biol.Chem., 275, 2000
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1E73
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![BU of 1e73 by Molmil](/molmil-images/mine/1e73) | 2-F-glucosylated MYROSINASE FROM SINAPIS ALBA with bound L-ascorbate | Descriptor: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-deoxy-2-fluoro-alpha-D-glucopyranose, ... | Authors: | Burmeister, W.P. | Deposit date: | 2000-08-23 | Release date: | 2001-01-05 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.5 Å) | Cite: | High Resolution X-Ray Crystallography Shows that Ascorbate is a Cofactor for Myrosinase and Substitutes for the Function of the Catalytic Base J.Biol.Chem., 275, 2000
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1E6X
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![BU of 1e6x by Molmil](/molmil-images/mine/1e6x) | MYROSINASE FROM SINAPIS ALBA with a bound transition state analogue,D-glucono-1,5-lactone | Descriptor: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, D-glucono-1,5-lactone, ... | Authors: | Burmeister, W.P. | Deposit date: | 2000-08-23 | Release date: | 2001-01-05 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.6 Å) | Cite: | High Resolution X-Ray Crystallography Shows that Ascorbate is a Cofactor for Myrosinase and Substitutes for the Function of the Catalytic Base J.Biol.Chem., 275, 2000
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