+Open data
-Basic information
Entry | Database: PDB / ID: 1clx | ||||||
---|---|---|---|---|---|---|---|
Title | CATALYTIC CORE OF XYLANASE A | ||||||
Components | XYLANASE A | ||||||
Keywords | XYLANASE / FAMILY-F XYLANASE FAMILY 10 GLYCOSYL-HYDROLASE | ||||||
Function / homology | Function and homology information cellulose binding / endo-1,4-beta-xylanase activity / endo-1,4-beta-xylanase / xylan catabolic process Similarity search - Function | ||||||
Biological species | Cellvibrio japonicus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.8 Å | ||||||
Authors | Harris, G.W. / Jenkins, J.A. / Connerton, I. / Pickersgill, R.W. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 1996 Title: Refined crystal structure of the catalytic domain of xylanase A from Pseudomonas fluorescens at 1.8 A resolution. Authors: Harris, G.W. / Jenkins, J.A. / Connerton, I. / Pickersgill, R.W. #1: Journal: FEBS Lett. / Year: 1995 Title: Beta-Glucosidase, Beta-Galactosidase, Family a Cellulases, Family F Xylanases and Two Barley Glycanases Form a Superfamily of Enzymes with 8-Fold Beta/Alpha Architecture and with Two Conserved ...Title: Beta-Glucosidase, Beta-Galactosidase, Family a Cellulases, Family F Xylanases and Two Barley Glycanases Form a Superfamily of Enzymes with 8-Fold Beta/Alpha Architecture and with Two Conserved Glutamates Near the Carboxy-Terminal Ends of Beta-Strands Four and Seven Authors: Jenkins, J. / Lo Leggio, L. / Harris, G. / Pickersgill, R. #2: Journal: Structure / Year: 1994 Title: Structure of the Catalytic Core of the Family F Xylanase from Pseudomonas Fluorescens and Identification of the Xylopentaose-Binding Sites Authors: Harris, G.W. / Jenkins, J.A. / Connerton, I. / Cummings, N. / Lo Leggio, L. / Scott, M. / Hazlewood, G.P. / Laurie, J.I. / Gilbert, H.J. / Pickersgill, R.W. #3: Journal: J.Mol.Biol. / Year: 1993 Title: Crystallization and Preliminary X-Ray Analysis of the Catalytic Domain of Xylanase a from Pseudomonas Fluorescens Subspecies Cellulosa Authors: Pickersgill, R.W. / Jenkins, J.A. / Scott, M. / Connerton, I. / Hazlewood, G.P. / Gilbert, H.J. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1clx.cif.gz | 291.7 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1clx.ent.gz | 243.1 KB | Display | PDB format |
PDBx/mmJSON format | 1clx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1clx_validation.pdf.gz | 392.5 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1clx_full_validation.pdf.gz | 432.8 KB | Display | |
Data in XML | 1clx_validation.xml.gz | 32.3 KB | Display | |
Data in CIF | 1clx_validation.cif.gz | 53.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cl/1clx ftp://data.pdbj.org/pub/pdb/validation_reports/cl/1clx | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
2 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 38460.477 Da / Num. of mol.: 4 / Fragment: CATALYTIC CORE, RESIDUES 264 - 611 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Cellvibrio japonicus (bacteria) / Strain: CELLULOSA / Gene: TRUNCATED XYNA (CODONS 264-611 / Plasmid: PET3A / Gene (production host): TRUNCATED XYNA (CODONS 264-611) / Production host: Escherichia coli (E. coli) / References: UniProt: P14768, endo-1,4-beta-xylanase #2: Chemical | ChemComp-CA / #3: Water | ChemComp-HOH / | Compound details | THE STRUCTURE IS OF THE CATALYTIC CORE OF XYLANASE A; THE COMPLETE XYLANASE WOULD ALSO CONSIST OF A ...THE STRUCTURE IS OF THE CATALYTIC CORE OF XYLANASE A; THE COMPLETE XYLANASE WOULD ALSO CONSIST OF A CELLULOSE BINDING DOMAIN AND A LINKER AS WELL AS THE CATALYTIC BINDING DOMAIN. A TRUNCATED GENE ENCODING THE CARBOXY-TERMINAL DOMAIN (I.E. THE CATALYTIC CORE) WAS EXPRESSED INDEPENDEN | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
---|
-Sample preparation
Crystal | Density Matthews: 2.29 Å3/Da / Density % sol: 46 % | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | pH: 7 / Details: pH 7.0 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 291 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: BL-6A / Wavelength: 0.92 |
Detector | Detector: IMAGE PLATE / Date: Jan 11, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Num. obs: 105167 / % possible obs: 78.8 % / Redundancy: 6.7 % / Rmerge(I) obs: 0.077 |
Reflection | *PLUS Highest resolution: 1.79 Å / Lowest resolution: 6.92 Å / Num. measured all: 703625 |
Reflection shell | *PLUS Highest resolution: 1.79 Å / Lowest resolution: 1.85 Å / % possible obs: 61.5 % / Num. unique obs: 7963 / Num. measured obs: 27549 / Rmerge(I) obs: 0.479 / Mean I/σ(I) obs: 1.5 |
-Processing
Software |
| ||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 1.8→10 Å / σ(F): 0 /
| ||||||||||||||||||
Displacement parameters | Biso mean: 16.6 Å2 | ||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
| ||||||||||||||||||
Software | *PLUS Name: RESTRAIN / Classification: refinement | ||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.166 | ||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||
Refine LS restraints | *PLUS
|