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Yorodumi- PDB-2nnl: Binding of two substrate analogue molecules to dihydroflavonol-4-... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2nnl | ||||||
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Title | Binding of two substrate analogue molecules to dihydroflavonol-4-reductase alters the functional geometry of the catalytic site | ||||||
Components | Dihydroflavonol 4-reductase | ||||||
Keywords | OXIDOREDUCTASE / ROSSMANN FOLD | ||||||
Function / homology | Function and homology information dihydroflavonol 4-reductase / dihydrokaempferol 4-reductase activity / flavanone 4-reductase activity / flavanone 4-reductase / anthocyanin-containing compound biosynthetic process / nucleotide binding Similarity search - Function | ||||||
Biological species | Vitis vinifera (wine grape) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Petit, P. / Langlois D'Estaintot, B. / Granier, T. / Gallois, B. | ||||||
Citation | Journal: To be Published Title: Binding of two substrate analogue molecules to dihydroflavonol-4-reductase alters the functional geometry of the catalytic site Authors: Petit, P. / Langlois D'Estaintot, B. / Granier, T. / Gallois, B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2nnl.cif.gz | 155 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2nnl.ent.gz | 120 KB | Display | PDB format |
PDBx/mmJSON format | 2nnl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2nnl_validation.pdf.gz | 1.5 MB | Display | wwPDB validaton report |
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Full document | 2nnl_full_validation.pdf.gz | 1.5 MB | Display | |
Data in XML | 2nnl_validation.xml.gz | 31.6 KB | Display | |
Data in CIF | 2nnl_validation.cif.gz | 46.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nn/2nnl ftp://data.pdbj.org/pub/pdb/validation_reports/nn/2nnl | HTTPS FTP |
-Related structure data
Related structure data | 2iodC 2c29S 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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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Refine code: 2
NCS ensembles :
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-Components
#1: Protein | Mass: 37694.344 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Vitis vinifera (wine grape) / Gene: dfr1 / Plasmid: PQE(30XA) / Production host: Escherichia coli (E. coli) / Strain (production host): M15(PREP4) References: UniProt: P93799, UniProt: P51110*PLUS, dihydroflavonol 4-reductase #2: Chemical | #3: Chemical | #4: 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: 2.45 Å3/Da / Density % sol: 49.76 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.9 Details: 50MM NACL, 29% PEG3350, 100MM HEPES, 3MM NAN3, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 1.04 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 5, 2005 / Details: mirrors |
Radiation | Monochromator: SI (311) MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.04 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→64.827 Å / Num. all: 37210 / Num. obs: 37210 / % possible obs: 85.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.4 % / Biso Wilson estimate: 34.4 Å2 / Rmerge(I) obs: 0.136 / Rsym value: 0.136 / Net I/σ(I): 3.7 |
Reflection shell | Resolution: 2.1→2.21 Å / Redundancy: 5.3 % / Mean I/σ(I) obs: 1.9 / Num. measured all: 29478 / Num. unique all: 5566 / % possible all: 89.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2c29 Resolution: 2.1→64.82 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.937 / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.291 / ESU R Free: 0.221 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 37.017 Å2
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Refine analyze | Luzzati coordinate error obs: 0.25 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→64.82 Å
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Refine LS restraints |
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Refine LS restraints NCS | Dom-ID: 1 / Auth asym-ID: D / Refine-ID: X-RAY DIFFRACTION
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LS refinement shell | Resolution: 2.1→2.155 Å / Total num. of bins used: 20
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