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- PDB-1ree: ENDO-1,4-BETA-XYLANASE II COMPLEX WITH 3,4-EPOXYBUTYL-BETA-D-XYLOSIDE -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ree | |||||||||
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Title | ENDO-1,4-BETA-XYLANASE II COMPLEX WITH 3,4-EPOXYBUTYL-BETA-D-XYLOSIDE | |||||||||
![]() | ENDO-1,4-BETA-XYLANASE II | |||||||||
![]() | HYDROLASE / XYLANASE / XYLAN DEGRADATION | |||||||||
Function / homology | ![]() endo-1,4-beta-xylanase activity / endo-1,4-beta-xylanase / xylan catabolic process / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Rouvinen, J. / Havukainen, R. / Torronen, A. | |||||||||
![]() | ![]() Title: Covalent binding of three epoxyalkyl xylosides to the active site of endo-1,4-xylanase II from Trichoderma reesei. Authors: Havukainen, R. / Torronen, A. / Laitinen, T. / Rouvinen, J. #1: ![]() Title: Three-Dimensional Structure of Endo-1,4-Beta-Xylanase II from Trichoderma Reesei: Two Conformational States in the Active Site Authors: Torronen, A. / Harkki, A. / Rouvinen, J. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 85.2 KB | Display | ![]() |
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PDB format | ![]() | 68.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.9869, -0.018, 0.1602), Vector: |
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Components
#1: Protein | Mass: 20838.436 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Sugar | ChemComp-07E / ( | #3: Chemical | ChemComp-BEZ / | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.27 Å3/Da / Density % sol: 45 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 4.2 / Method: vapor diffusion, hanging drop / Details: Torronen, A., (1993) J. Mol. Biol., 233, 313. | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Jul 18, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 35521 / % possible obs: 85.1 % / Observed criterion σ(I): 1 / Redundancy: 2.4 % / Rmerge(I) obs: 0.0907 |
Reflection | *PLUS Highest resolution: 1.7 Å / Num. measured all: 84926 |
Reflection shell | *PLUS Highest resolution: 1.7 Å / Lowest resolution: 1.8 Å / % possible obs: 57.5 % |
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Processing
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Refinement | Resolution: 1.6→8 Å / σ(F): 1
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Displacement parameters | Biso mean: 21.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.6→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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