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Open data
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Basic information
Entry | Database: PDB / ID: 1m4w | |||||||||
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Title | Thermophilic b-1,4-xylanase from Nonomuraea flexuosa | |||||||||
![]() | endoxylanase | |||||||||
![]() | HYDROLASE / xylanase / glycosyl hydrolase / family 11 / thermostability | |||||||||
Function / homology | ![]() polysaccharide binding / endo-1,4-beta-xylanase activity / endo-1,4-beta-xylanase / xylan catabolic process Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Hakulinen, N. / Turunen, O. / Janis, J. / Leisola, M. / Rouvinen, J. | |||||||||
![]() | ![]() Title: Three-dimensional structures of thermophilic beta-1,4-xylanases from Chaetomium thermophilum and Nonomuraea flexuosa. Comparison of twelve xylanases in relation to their thermal stability. Authors: Hakulinen, N. / Turunen, O. / Leisola, M. / Rouvinen, J. | |||||||||
History |
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Remark 999 | SEQUENCE At the time of processing, there was no database sequence available for this protein. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 53.4 KB | Display | ![]() |
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PDB format | ![]() | 40 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 739.3 KB | Display | ![]() |
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Full document | ![]() | 740.8 KB | Display | |
Data in XML | ![]() | 11.8 KB | Display | |
Data in CIF | ![]() | 16.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1h1aC ![]() 1enxS 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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1 |
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Unit cell |
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Components
#1: Protein | Mass: 21802.447 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: GenBank: 23337128, UniProt: Q8GMV7*PLUS, endo-1,4-beta-xylanase |
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#2: Polysaccharide | alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
#3: Chemical | ChemComp-ACT / |
#4: Chemical | ChemComp-GOL / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6 Details: 0.8 M Ammonium sulphate, 0.1 M Sodium Acetate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Oct 20, 2000 / Details: MSC Confocal Blue |
Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→99 Å / Num. obs: 8541 / % possible obs: 97.6 % / Redundancy: 5.7 % / Biso Wilson estimate: 23 Å2 / Rsym value: 0.107 / Net I/σ(I): 17.9 |
Reflection shell | Resolution: 2.1→2.18 Å / Rsym value: 0.293 / % possible all: 92.8 |
Reflection | *PLUS Num. measured all: 48587 / Rmerge(I) obs: 0.107 |
Reflection shell | *PLUS % possible obs: 92.8 % / Rmerge(I) obs: 0.293 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1ENX Resolution: 2.1→99 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.1→99 Å
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Refine LS restraints |
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Refine LS restraints | *PLUS
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