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Open data
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Basic information
Entry | Database: PDB / ID: 1ex1 | |||||||||
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Title | BETA-D-GLUCAN EXOHYDROLASE FROM BARLEY | |||||||||
![]() | PROTEIN (BETA-D-GLUCAN EXOHYDROLASE ISOENZYME EXO1) | |||||||||
![]() | HYDROLASE / CELL WALL DEGRADATION | |||||||||
Function / homology | ![]() glucan catabolic process / beta-glucosidase / beta-glucosidase activity / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Varghese, J.N. / Hrmova, M. / Fincher, G.B. | |||||||||
![]() | ![]() Title: Three-dimensional structure of a barley beta-D-glucan exohydrolase, a family 3 glycosyl hydrolase. Authors: Varghese, J.N. / Hrmova, M. / Fincher, G.B. #1: ![]() Title: Crystallization and Preliminary X-Ray Analysis of Beta-D-Glucan Exohydrolase Isoenzyme Exo1 from Barley (Hordeum Vulgare); a Family 3 Glycosyl Hydrolase Authors: Varghese, J.N. / Hrmova, M. / Hoj, P.B. / Fincher, G.B. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 132.6 KB | Display | ![]() |
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PDB format | ![]() | 102.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 901.6 KB | Display | ![]() |
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Full document | ![]() | 916.1 KB | Display | |
Data in XML | ![]() | 27 KB | Display | |
Data in CIF | ![]() | 37.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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Components
#1: Protein | Mass: 65475.617 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: THREE GLYCSYLATED SITES AT ASN 221, 498, 600 GLUCOSE BOUND IN PUTATIVE ACTIVE SITE Source: (natural) ![]() ![]() References: GenBank: AAD23382, UniProt: Q9XEI3*PLUS, glucan 1,3-beta-glucosidase |
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#2: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-D-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
#3: Sugar | ChemComp-NAG / |
#4: Sugar | ChemComp-GLC / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.83 Å3/Da / Density % sol: 66 % Description: THE SAME CRYSTAL WAS USED TO COLLECT BOTH NATIVE AND PIP DATA | ||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7 / Details: pH 7.0 | ||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 277-279 K / Method: vapor diffusion, hanging drop / Details: Hrmova, M., (1998) Acta Cryst., D54, 687. | ||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 291 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: May 15, 1997 / Details: MIRRORS |
Radiation | Monochromator: NI FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→20 Å / Num. obs: 408526 / % possible obs: 78 % / Observed criterion σ(I): 1 / Redundancy: 2.5 % / Biso Wilson estimate: 26.6 Å2 / Rmerge(I) obs: 0.054 / Net I/σ(I): 20.1 |
Reflection shell | Resolution: 2.2→2.3 Å / Rmerge(I) obs: 0.142 / Mean I/σ(I) obs: 2.8 / % possible all: 37.8 |
Reflection | *PLUS Num. obs: 40310 / Observed criterion σ(I): 1 / Redundancy: 3.7 % / Num. measured all: 148526 |
Reflection shell | *PLUS % possible obs: 32 % |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 2.2→20 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.2 Å / σ(F): 1 / % reflection Rfree: 5 % / Rfactor obs: 0.17 / Rfactor Rwork: 0.17 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.283 / Rfactor Rwork: 0.202 / Num. reflection obs: 1633 / Rfactor obs: 0.202 |