+Open data
-Basic information
Entry | Database: PDB / ID: 1axk | ||||||
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Title | ENGINEERED BACILLUS BIFUNCTIONAL ENZYME GLUXYN-1 | ||||||
Components | GLUXYN-1 | ||||||
Keywords | FUSION PROTEIN / GLUXYN-1 / BIFUNCTIONAL / 1 / 4-BETA-XYLANASE / 3-1 / 4-BETA-GLUCANASE / HYBRID ENZYME | ||||||
Function / homology | Function and homology information licheninase activity / licheninase / endo-1,4-beta-xylanase activity / endo-1,4-beta-xylanase / xylan catabolic process / carbohydrate metabolic process Similarity search - Function | ||||||
Biological species | Bacillus subtilis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Ay, J. / Heinemann, U. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1998 Title: Structure and function of the Bacillus hybrid enzyme GluXyn-1: native-like jellyroll fold preserved after insertion of autonomous globular domain. Authors: Ay, J. / Gotz, F. / Borriss, R. / Heinemann, U. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1axk.cif.gz | 166.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1axk.ent.gz | 133.8 KB | Display | PDB format |
PDBx/mmJSON format | 1axk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ax/1axk ftp://data.pdbj.org/pub/pdb/validation_reports/ax/1axk | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 43812.676 Da / Num. of mol.: 2 Fragment: FUSION OF 1,3-1,4-BETA-GLUCANASE DOMAIN AND 1,4-BETA-XYLANASE DOMAIN Source method: isolated from a genetically manipulated source Details: ACTIVE AS BOTH A 1,3-1,4-BETA-GLUCANASE AND A 1,4-BETA-XYLANASE Source: (gene. exp.) Bacillus subtilis (bacteria) / Cell line: DH5-ALPHA / Fragment: 1,4-BETA-XYLANASE DOMAIN / Plasmid: PFD1 / Cell line (production host): DH5-ALPHA / Production host: Escherichia coli (E. coli) References: UniProt: P23904, UniProt: P18429, licheninase, endo-1,4-beta-xylanase #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 46.4 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 8.5 / Details: pH 8.5 | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8.7 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 123 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 1.008 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Aug 1, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.008 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→20 Å / Num. obs: 48499 / % possible obs: 91.3 % / Observed criterion σ(I): 0 / Redundancy: 3.4 % / Biso Wilson estimate: 23.98 Å2 / Rmerge(I) obs: 0.058 / Rsym value: 0.058 / Net I/σ(I): 11.6 |
Reflection shell | Resolution: 2.1→2.21 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.23 / Mean I/σ(I) obs: 3.3 / Rsym value: 0.23 / % possible all: 80 |
Reflection | *PLUS Num. measured all: 165157 |
Reflection shell | *PLUS Lowest resolution: 2.17 Å / % possible obs: 80 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: CIRCULARLY PERMUTED 1,3-1,4-ENDO-BETA-GLUCANASE CPMAC57 (PDB ENTRY 1CPN) AND BACILLUS CIRCULANS 1,3-ENDO-BETA-XYLANASE (PDB ENTRY 1BCX). Resolution: 2.1→19.96 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 21.7 Å2
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Refine analyze | Luzzati coordinate error obs: 0.3 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→19.96 Å
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Refine LS restraints |
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