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Open data
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Basic information
Entry | Database: PDB / ID: 5eau | ||||||
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Title | 5-EPI-ARISTOLOCHENE SYNTHASE FROM NICOTIANA TABACUM | ||||||
![]() | 5-EPI-ARISTOLOCHENE SYNTHASE | ||||||
![]() | ISOPRENOID SYNTHASE / 5-EPI-ARISTOLOCHENE SYNTHASE / NATURAL PRODUCTS BIOSYNTHESIS / ISOPRENOID CYCLASE | ||||||
Function / homology | ![]() 5-epiaristolochene synthase / 5-epi-aristolochene synthase activity / sesquiterpene biosynthetic process / diterpenoid biosynthetic process / terpene synthase activity / magnesium ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Starks, C.M. / Back, K. / Chappell, J. / Noel, J.P. | ||||||
![]() | ![]() Title: Structural basis for cyclic terpene biosynthesis by tobacco 5-epi-aristolochene synthase. Authors: Starks, C.M. / Back, K. / Chappell, J. / Noel, J.P. #1: ![]() Title: Expression of a Plant Sesquiterpene Cyclase Gene in Escherichia Coli Authors: Back, K. / Yin, S. / Chappell, J. #2: ![]() Title: Purification and Characterization of an Inducible Sesquiterpene Cyclase from Elicitor-Treated Tobacco Cell Suspension Cultures Authors: Vogeli, U. / Freeman, J.W. / Chappell, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 120.9 KB | Display | ![]() |
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PDB format | ![]() | 93.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 894 KB | Display | ![]() |
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Full document | ![]() | 900.9 KB | Display | |
Data in XML | ![]() | 21.7 KB | Display | |
Data in CIF | ![]() | 30.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5easSC ![]() 5eatC S: Starting model for refinement C: citing same article ( |
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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: 63043.484 Da / Num. of mol.: 1 / Mutation: EXPRESSED WITH 6-HIS TAG Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
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#2: Chemical | #3: Chemical | ChemComp-FFF / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.87 Å3/Da / Density % sol: 68 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.9 Details: PROTEIN WAS CRYSTALLIZED FROM 15% PEG 8000, 200 MM MG(OAC)2, 100 MM MOPSO PH 6.9, 1MM DTT; SOAKING SOLUTION FOR FREEZING ALSO INCLUDED 20% ETHYLENE GLYCOL. | ||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 90 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 1, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.08 Å / Relative weight: 1 |
Reflection | Resolution: 2.16→23.3 Å / Num. obs: 49688 / % possible obs: 91.5 % / Observed criterion σ(I): -2 / Redundancy: 5.4 % / Rsym value: 0.052 / Net I/σ(I): 8 |
Reflection shell | Resolution: 2.15→2.2 Å / Redundancy: 3.8 % / Mean I/σ(I) obs: 2.7 / Rsym value: 0.444 / % possible all: 70.3 |
Reflection | *PLUS Num. measured all: 268076 / Rmerge(I) obs: 0.076 |
Reflection shell | *PLUS % possible obs: 70.3 % / Rmerge(I) obs: 0.469 |
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Processing
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Refinement | Method to determine structure: DIFFERENCE FOURIER Starting model: PDB ENTRY 5EAS Resolution: 2.15→22 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT Details: THE PROTEIN CONSISTS OF RESIDUES 1 - 548. RESIDUES 1 - 20 ARE ABSENT FROM THE ELECTRON DENSITY. RESIDUES 97 - 102 EXHIBIT WEAK DENSITY, AND MAY BE IN MULTIPLE CONFORMATIONS. RESIDUES 315 - ...Details: THE PROTEIN CONSISTS OF RESIDUES 1 - 548. RESIDUES 1 - 20 ARE ABSENT FROM THE ELECTRON DENSITY. RESIDUES 97 - 102 EXHIBIT WEAK DENSITY, AND MAY BE IN MULTIPLE CONFORMATIONS. RESIDUES 315 - 333 EXHIBIT ANISOTROPIC ELECTRON DENSITY. RESIDUES 524 - 528 ARE ABSENT FROM THE ELECTRON DENSITY. MUCH OF THE FARNESYL CHAIN OF THE BOUND SUBSTRATE ANALOG IS DISORDERED.
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Displacement parameters | Biso mean: 40.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.15→22 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.15→2.25 Å / Rfactor Rfree error: 0.03 / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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