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Yorodumi- PDB-3zok: Structure of 3-Dehydroquinate Synthase from Actinidia chinensis i... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3zok | ||||||
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Title | Structure of 3-Dehydroquinate Synthase from Actinidia chinensis in complex with NAD | ||||||
Components | 3-DEHYDROQUINATE SYNTHASE | ||||||
Keywords | LYASE / SHIKIMATE PATHWAY | ||||||
Function / homology | Function and homology information chorismate biosynthetic process => GO:0009423 / 3-dehydroquinate synthase / 3-dehydroquinate synthase activity / chorismate biosynthetic process / aromatic amino acid family biosynthetic process / chloroplast / NAD binding / identical protein binding / metal ion binding Similarity search - Function | ||||||
Biological species | ACTINIDIA CHINENSIS (golden kiwifruit) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Mittelstaedt, G. / Negron, L. / Schofield, L.R. / Marsh, K. / Parker, E.J. | ||||||
Citation | Journal: Arch. Biochem. Biophys. / Year: 2013 Title: Biochemical and structural characterisation of dehydroquinate synthase from the New Zealand kiwifruit Actinidia chinensis. Authors: Mittelstadt, G. / Negron, L. / Schofield, L.R. / Marsh, K. / Parker, E.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3zok.cif.gz | 291.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3zok.ent.gz | 235.2 KB | Display | PDB format |
PDBx/mmJSON format | 3zok.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zo/3zok ftp://data.pdbj.org/pub/pdb/validation_reports/zo/3zok | HTTPS FTP |
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-Related structure data
Related structure data | 1nr5S S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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-Components
-Protein , 1 types, 4 molecules ABCD
#1: Protein | Mass: 41144.160 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ACTINIDIA CHINENSIS (golden kiwifruit) / Plasmid: PET200/ACHDHQS / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA2 / References: UniProt: U3KRF2*PLUS, 3-dehydroquinate synthase |
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-Non-polymers , 8 types, 212 molecules
#2: Chemical | ChemComp-PO4 / #3: Chemical | ChemComp-NAD / #4: Chemical | ChemComp-PEG / #5: Chemical | ChemComp-GLY / #6: Chemical | ChemComp-2PE / | #7: Chemical | ChemComp-PGE / | #8: Chemical | ChemComp-PG4 / | #9: Water | ChemComp-HOH / | |
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-Details
Nonpolymer details | NONAETHYLENE GLYCOL (2PE): 2PE MONOMER WAS ADDED BUT SHORTENED BY ONE ETHYLENE GLYCOL UNIT, THE ...NONAETHYLE |
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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: 2.22 Å3/Da / Density % sol: 44.66 % / Description: NONE |
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Crystal grow | pH: 7 Details: 0.1 M SPG BUFFER (PH 7.0), 25% PEG 1500, 0.25 MM COCL2, 0.0003 MM NAD |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.97948 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Oct 19, 2011 |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97948 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→50.32 Å / Num. obs: 55631 / % possible obs: 99.6 % / Observed criterion σ(I): 2 / Redundancy: 4.4 % / Rmerge(I) obs: 0.12 / Net I/σ(I): 9.2 |
Reflection shell | Resolution: 2.4→2.53 Å / Redundancy: 4.5 % / Rmerge(I) obs: 0.42 / Mean I/σ(I) obs: 3.1 / % possible all: 99.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1NR5 Resolution: 2.4→45.5 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.902 / SU B: 8.82 / SU ML: 0.206 / Cross valid method: THROUGHOUT / ESU R: 0.602 / ESU R Free: 0.289 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 33.021 Å2
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Refinement step | Cycle: LAST / Resolution: 2.4→45.5 Å
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Refine LS restraints |
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