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Yorodumi- PDB-2hxt: Crystal structure of L-Fuconate Dehydratase from Xanthomonas camp... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2hxt | ||||||
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Title | Crystal structure of L-Fuconate Dehydratase from Xanthomonas campestris liganded with Mg++ and D-erythronohydroxamate | ||||||
Components | L-fuconate dehydratase | ||||||
Keywords | UNKNOWN FUNCTION / L-fuconate dehydratase / enolase superfamily / D-erythromohydroxamate | ||||||
Function / homology | Function and homology information L-fuconate dehydratase / L-fuconate dehydratase activity / hydro-lyase activity / carbohydrate catabolic process / magnesium ion binding Similarity search - Function | ||||||
Biological species | Xanthomonas campestris pv. campestris (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Fedorov, A.A. / Fedorov, E.V. / Yew, W.S. / Rakus, J.F. / Gerlt, J.A. / Almo, S.C. | ||||||
Citation | Journal: Biochemistry / Year: 2006 Title: Evolution of Enzymatic Activities in the Enolase Superfamily: l-Fuconate Dehydratase from Xanthomonas campestris. Authors: Yew, W.S. / Fedorov, A.A. / Fedorov, E.V. / Rakus, J.F. / Pierce, R.W. / Almo, S.C. / Gerlt, J.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2hxt.cif.gz | 107 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2hxt.ent.gz | 79.9 KB | Display | PDB format |
PDBx/mmJSON format | 2hxt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2hxt_validation.pdf.gz | 439.3 KB | Display | wwPDB validaton report |
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Full document | 2hxt_full_validation.pdf.gz | 441.7 KB | Display | |
Data in XML | 2hxt_validation.xml.gz | 20.9 KB | Display | |
Data in CIF | 2hxt_validation.cif.gz | 32.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hx/2hxt ftp://data.pdbj.org/pub/pdb/validation_reports/hx/2hxt | HTTPS FTP |
-Related structure data
Related structure data | 2hxuC 2hneS 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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Unit cell |
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Details | The biological assembly is a dimer, generated from the monomer in the asymmetric unit by crystallographic two fold axis |
-Components
#1: Protein | Mass: 48178.617 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Xanthomonas campestris pv. campestris (bacteria) Species: Xanthomonas campestris / Strain: ATCC 33913 / Production host: Escherichia coli (E. coli) / References: UniProt: Q8P3K2 |
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#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-EHM / ( |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.89 Å3/Da / Density % sol: 68.38 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 56% Tacsimate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X4A / Wavelength: 0.97911 Å |
Detector | Type: ADSC / Detector: CCD / Date: Apr 15, 2006 |
Radiation | Monochromator: Double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97911 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→24.8 Å / Num. all: 82705 / Num. obs: 82705 / % possible obs: 98.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 1.7→1.76 Å / % possible all: 93.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2HNE Resolution: 1.7→24.8 Å / σ(F): 0.8 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.7→24.8 Å
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Refine LS restraints |
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