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- PDB-1goq: Thermostable xylanase I from Thermoascus aurantiacus - Room tempe... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1goq | ||||||||||||
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Title | Thermostable xylanase I from Thermoascus aurantiacus - Room temperature xylobiose complex | ||||||||||||
![]() | ENDO-1,4-BETA-XYLANASE | ||||||||||||
![]() | HYDROLASE / XYLANASE / FAMILY 10 / PLANT CELL WALL DEGRADATION | ||||||||||||
Function / homology | ![]() endo-1,4-beta-xylanase activity / endo-1,4-beta-xylanase / xylan catabolic process Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | ![]() ![]() | ||||||||||||
![]() | Lo Leggio, L. / Larsen, S. | ||||||||||||
![]() | ![]() Title: Substrate Specificity and Subsite Mobility in T. Aurantiacus Xylanase 10A Authors: Lo Leggio, L. / Kalogiannis, S. / Eckert, K. / Teixeira, S.C.M. / Bhat, M.K. / Andrei, C. / Pickersgill, R.W. / Larsen, S. #1: Journal: Acta Crystallogr.,Sect.D / Year: 2001 Title: Anisotropic Refinement of the Structure of Thermoascus Aurantiacus Xylanase I Authors: Teixeira, S. / Lo Leggio, L. / Pickersgill, R. / Cardin, C. #2: Journal: Proteins / Year: 1999 Title: High Resolution Structure and Sequence of T. Aurantiacus Xylanase I: Implications for the Evolution of Thermostability in Family 10 Xylanases and Enzymes with Beta/Alpha Barrel Architecture Authors: Lo Leggio, L. / Kalogiannis, S. / Bhat, M.K. / Pickersgill, R.W. #3: Journal: Biochem.Soc.Trans. / Year: 1998 Title: Superfamilies: The 4/7 Superfamily of Beta/ Alpha-Barrel Glycosidases and the Right-Handed Parallel Beta-Helix Superfamily Authors: Pickersgill, R. / Harris, G. / Lo Leggio, L. / Mayans, O. / Jenkins, J. #4: ![]() Title: Structure Solution of Thermoascus Aurantiacus Xylanase. Structural Studies of Xylanases and Endoglucanases Authors: Lo Leggio, L. | ||||||||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 76.7 KB | Display | ![]() |
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PDB format | ![]() | 54.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 14.2 KB | Display | |
Data in CIF | ![]() | 19.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1gokSC ![]() 1gomC ![]() 1gooC ![]() 1gorC ![]() 1k6aC C: citing same article ( S: Starting model for refinement |
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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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Components
#1: Protein | Mass: 32890.711 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() | ||||||
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#2: Polysaccharide | #3: Sugar | #4: Water | ChemComp-HOH / | Sequence details | RESIDUES 1-26 REFER TO THE SIGNAL PEPTIDE IT IS NOT KNOWN IF GLN 303 IS PRESENT IN THE CRYSTAL | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.02 Å3/Da / Density % sol: 32.9 % / Description: THE PH OF CRYSTALLIZATION WAS NOT BUFFERED |
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 7 Details: HANGING DROPS CONTAINING 1:1 RATIO OF 20-30 MG/ML PROTEIN SOLUTION AND RESERVOIR SOLUTION (12 % TO 25 % PEG 6,000). THE CRYSTAL WAS SOAKED IN 0.5 M XYLOBIOSE, pH 7.00 |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: R-AXIS / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→30 Å / Num. obs: 20709 / % possible obs: 86 % / Observed criterion σ(I): 0 / Redundancy: 6.4 % / Rmerge(I) obs: 0.17 |
Reflection shell | Resolution: 1.8→1.83 Å / Redundancy: 4.3 % / Rmerge(I) obs: 0.338 / % possible all: 37.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1GOK Resolution: 1.8→5 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 100000 / Data cutoff low absF: 0.1 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 18.8 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.8→5 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.8→1.91 Å / Rfactor Rfree error: 0.02 / Total num. of bins used: 6
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Xplor file |
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