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Yorodumi- PDB-2e4o: X-ray Crystal Structure of Aristolochene Synthase from Aspergillu... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2e4o | ||||||
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Title | X-ray Crystal Structure of Aristolochene Synthase from Aspergillus terreus and the Evolution of Templates for the Cyclization of Farnesyl Diphosphate | ||||||
Components | Aristolochene synthase | ||||||
Keywords | LYASE / sesquiterpene cyclase / farnesyl diphosphate | ||||||
Function / homology | Function and homology information aristolochene synthase / aristolochene synthase activity / small molecule metabolic process / metal ion binding Similarity search - Function | ||||||
Biological species | Aspergillus terreus (mold) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å | ||||||
Authors | Shishova, E.Y. / Di Costanzo, L. / Cane, D.E. / Christianson, D.W. | ||||||
Citation | Journal: Biochemistry / Year: 2007 Title: X-ray crystal structure of aristolochene synthase from Aspergillus terreus and evolution of templates for the cyclization of farnesyl diphosphate. Authors: Shishova, E.Y. / Di Costanzo, L. / Cane, D.E. / Christianson, D.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2e4o.cif.gz | 246.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2e4o.ent.gz | 200 KB | Display | PDB format |
PDBx/mmJSON format | 2e4o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2e4o_validation.pdf.gz | 487.8 KB | Display | wwPDB validaton report |
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Full document | 2e4o_full_validation.pdf.gz | 525.8 KB | Display | |
Data in XML | 2e4o_validation.xml.gz | 46.5 KB | Display | |
Data in CIF | 2e4o_validation.cif.gz | 63.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e4/2e4o ftp://data.pdbj.org/pub/pdb/validation_reports/e4/2e4o | HTTPS FTP |
-Related structure data
Related structure data | 2oa6C 1di1S 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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-Components
#1: Protein | Mass: 36523.715 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aspergillus terreus (mold) / Gene: Ari1 / Plasmid: pET11a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: Q9UR08, aristolochene synthase #2: Chemical | ChemComp-BME / #3: Chemical | #4: Chemical | ChemComp-MES / | #5: 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: 2.56 Å3/Da / Density % sol: 51.88 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 100mM Tris, 18% PEG 6000, 0.5M NaCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 6, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→50 Å / Num. all: 73132 / Num. obs: 72129 / % possible obs: 96.2 % / Observed criterion σ(I): 2.3 / Redundancy: 2.9 % / Biso Wilson estimate: 36.7 Å2 / Rmerge(I) obs: 0.084 / Net I/σ(I): 19 |
Reflection shell | Resolution: 2.2→2.28 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.534 / Mean I/σ(I) obs: 2.26 / Num. unique all: 6773 / % possible all: 89.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1DI1 Resolution: 2.2→50 Å / Cross valid method: THROUGHOUT / Stereochemistry target values: cns library
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Refinement step | Cycle: LAST / Resolution: 2.2→50 Å
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Refine LS restraints |
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