+Open data
-Basic information
Entry | Database: PDB / ID: 1h1a | |||||||||
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Title | Thermophilic beta-1,4-xylanase from Chaetomium thermophilum | |||||||||
Components | Endo-1,4-beta-xylanaseXylanase | |||||||||
Keywords | HYDROLASE / XYLANASE / GLYCOSYL HYDROLASE / FAMILY 11 / THERMOSTABILITY GLYCOSIDASE | |||||||||
Function / homology | Function and homology information endo-1,4-beta-xylanase activity / endo-1,4-beta-xylanase / xylan catabolic process Similarity search - Function | |||||||||
Biological species | Chaetomium thermophilum (fungus) | |||||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.75 Å | |||||||||
Authors | Hakulinen, N. / Rouvinen, J. | |||||||||
Citation | Journal: Eur.J.Biochem. / Year: 2003 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. / Janis, J. / Leisola, M. / Rouvinen, J. | |||||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1h1a.cif.gz | 101.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1h1a.ent.gz | 76.8 KB | Display | PDB format |
PDBx/mmJSON format | 1h1a.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/h1/1h1a ftp://data.pdbj.org/pub/pdb/validation_reports/h1/1h1a | HTTPS FTP |
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-Related structure data
Related structure data | 1m4wC 1enxS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Components on special symmetry positions |
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-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 21090.709 Da / Num. of mol.: 2 / Fragment: CATALYTIC DOMAIN, RESIDUES 27-217 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Chaetomium thermophilum (fungus) / Gene: xyn11A / Production host: TRICHODERMA REESEI (fungus) / References: UniProt: Q8J1V6, endo-1,4-beta-xylanase |
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-Non-polymers , 5 types, 609 molecules
#2: Chemical | #3: Chemical | #4: Chemical | ChemComp-CA / | #5: Chemical | ChemComp-GOL / | #6: Water | ChemComp-HOH / | |
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-Details
Nonpolymer details | THE RESIDUES A1193 AND B1193 WERE ORIGINALLY DEPOSITED AS ISOLATED SULFUR ATOMS. AS PART OF ...THE RESIDUES A1193 AND B1193 WERE ORIGINALLY |
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Sequence details | THE N-TERMINAL RESIDUE (PCA 1) IS A PYROGLUTAM |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.41 Å3/Da / Density % sol: 48.92 % | ||||||||||||||||||||||||
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Crystal grow | pH: 7.2 / Details: 1.4 M AMMONIUM SULPHATE, 0.1 M HEPES, PH 7.2 | ||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.2 / 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: ROTATING ANODE / Type: RIGAKU RU200HB / Wavelength: 1.5418 |
Detector | Type: RIGAKU IMAGE PLATE / Detector: IMAGE PLATE / Date: Aug 15, 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: 1.75→99 Å / Num. obs: 40787 / % possible obs: 97.3 % / Redundancy: 4.7 % / Biso Wilson estimate: 18.2 Å2 / Rmerge(I) obs: 0.077 / Net I/σ(I): 27.1 |
Reflection shell | Resolution: 1.75→1.81 Å / Rmerge(I) obs: 0.302 / % possible all: 90.9 |
Reflection | *PLUS Highest resolution: 1.75 Å / Lowest resolution: 99 Å / Num. measured all: 190677 / Rmerge(I) obs: 0.077 |
Reflection shell | *PLUS % possible obs: 90.9 % / Rmerge(I) obs: 0.302 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1ENX Resolution: 1.75→99 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 20.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.75→99 Å
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Refine LS restraints |
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