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- PDB-1e4l: Crystal structure of the inactive mutant Monocot (Maize ZMGlu1) b... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1e4l | ||||||
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Title | Crystal structure of the inactive mutant Monocot (Maize ZMGlu1) beta-glucosidase ZM Glu191Asp | ||||||
![]() | BETA-GLUCOSIDASE, CHLOROPLASTIC | ||||||
![]() | HYDROLASE / GLYCOSIDE HYDROLASE / FAMILY 1 / RETENTION OF THE ANOMERIC CONFIGURATION / INACTIVE MUTANT E191D | ||||||
Function / homology | ![]() galactosidase activity / fucosidase activity / xylanase activity / 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase / DIMBOA glucoside beta-D-glucosidase activity / cytokinin-activated signaling pathway / mannosidase activity / cellulose 1,4-beta-cellobiosidase activity / scopolin beta-glucosidase activity / beta-glucosidase ...galactosidase activity / fucosidase activity / xylanase activity / 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase / DIMBOA glucoside beta-D-glucosidase activity / cytokinin-activated signaling pathway / mannosidase activity / cellulose 1,4-beta-cellobiosidase activity / scopolin beta-glucosidase activity / beta-glucosidase / beta-glucosidase activity / chloroplast / carbohydrate metabolic process Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Czjzek, M. / Cicek, M. / Bevan, D.R. / Henrissat, B. / Esen, A. | ||||||
![]() | ![]() Title: The Mechanism of Substrate (Aglycone) Specificity in Beta -Glucosidases is Revealed by Crystal Structures of Mutant Maize Beta -Glucosidase-Dimboa, -Dimboaglc, and -Dhurrin Complexes Authors: Czjzek, M. / Cicek, M. / Zamboni, V. / Bevan, D.R. / Henrissat, B. / Esen, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 206.3 KB | Display | ![]() |
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PDB format | ![]() | 165.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 440.5 KB | Display | ![]() |
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Full document | ![]() | 456.1 KB | Display | |
Data in XML | ![]() | 40.1 KB | Display | |
Data in CIF | ![]() | 56.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1e4nC ![]() 1e55C ![]() 1e56C ![]() 1e1eS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.8236, 0.36629, -0.43302), Vector: |
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Components
#1: Protein | Mass: 58458.422 Da / Num. of mol.: 2 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | Compound details | ENGINEERED | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.21 Å3/Da / Density % sol: 44.43 % | ||||||||||||||||||||
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Crystal grow | pH: 7.5 / Details: 22 % PEG 4000, 5 % ISOPROPANOL, 0.1 M HEPES PH 7.5 | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Date: Mar 15, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.93 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→19.9 Å / Num. obs: 549492 / % possible obs: 98.3 % / Redundancy: 3.1 % / Rmerge(I) obs: 0.043 / Rsym value: 0.036 / Net I/σ(I): 14.2 |
Reflection shell | Resolution: 2.2→2.26 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.141 / Mean I/σ(I) obs: 2.4 / Rsym value: 0.113 / % possible all: 96.4 |
Reflection shell | *PLUS % possible obs: 96.4 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1E1E Resolution: 2.2→19 Å / Data cutoff high absF: 1000000 / Cross valid method: THROUGHOUT / σ(F): 0.1 Details: THE N- AND C-TERMINAL RESIDUES WERE NOT SEEN IN THE ELECTRON DENSITY MAPS
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 37.5 Å2 / ksol: 0.3682 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 21.33 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.2→19 Å
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Refine LS restraints |
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Refine LS restraints NCS | Rms dev position: 0.305 Å / Weight position: 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.2→2.28 Å / Total num. of bins used: 10
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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