+Open data
-Basic information
Entry | Database: PDB / ID: 5gp0 | ||||||
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Title | Crystal structure of geraniol-NUDX1 complex | ||||||
Components | Nudix hydrolase 1 | ||||||
Keywords | HYDROLASE / geraniol / NUDX1 / Arabidopsis thaliana / complex | ||||||
Function / homology | Function and homology information dihydroneopterin triphosphate diphosphatase / dihydroneopterin triphosphate pyrophosphohydrolase activity / NAD+ diphosphatase / NAD+ diphosphatase activity / NADH pyrophosphatase activity / 8-oxo-dGTP diphosphatase / dGTP catabolic process / 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity / 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity / DNA damage response ...dihydroneopterin triphosphate diphosphatase / dihydroneopterin triphosphate pyrophosphohydrolase activity / NAD+ diphosphatase / NAD+ diphosphatase activity / NADH pyrophosphatase activity / 8-oxo-dGTP diphosphatase / dGTP catabolic process / 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity / 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity / DNA damage response / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | Arabidopsis thaliana (thale cress) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.702 Å | ||||||
Authors | Liu, J. / Guan, Z. / Zou, T. / Yin, P. | ||||||
Citation | Journal: Mol Plant / Year: 2018 Title: Structural Insights into the Substrate Recognition Mechanism of Arabidopsis GPP-Bound NUDX1 for Noncanonical Monoterpene Biosynthesis. Authors: Liu, J. / Guan, Z. / Liu, H. / Qi, L. / Zhang, D. / Zou, T. / Yin, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5gp0.cif.gz | 246 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5gp0.ent.gz | 198.1 KB | Display | PDB format |
PDBx/mmJSON format | 5gp0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5gp0_validation.pdf.gz | 2.5 MB | Display | wwPDB validaton report |
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Full document | 5gp0_full_validation.pdf.gz | 2.5 MB | Display | |
Data in XML | 5gp0_validation.xml.gz | 32.2 KB | Display | |
Data in CIF | 5gp0_validation.cif.gz | 45.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gp/5gp0 ftp://data.pdbj.org/pub/pdb/validation_reports/gp/5gp0 | HTTPS FTP |
-Related structure data
Related structure data | 5wwdC 5wy6C 4kyxS 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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2 |
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3 |
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Unit cell |
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-Components
#1: Protein | Mass: 16582.779 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: NUDT1, NUDX1, At1g68760, F14K14.13 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) References: UniProt: Q9CA40, 8-oxo-dGTP diphosphatase, dihydroneopterin triphosphate diphosphatase, NAD+ diphosphatase #2: Chemical | #3: Chemical | ChemComp-GPP / #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: 2.51 Å3/Da / Density % sol: 50.92 % |
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Crystal grow | Temperature: 291.15 K / Method: vapor diffusion, hanging drop Details: Sodium acetate trihydrate, PEG 2000, Ammonium sulfate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.9793 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Apr 5, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9793 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→50 Å / Num. obs: 75230 / % possible obs: 99.9 % / Redundancy: 7.1 % / Net I/σ(I): 15.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4KYX Resolution: 1.702→44.681 Å / SU ML: 0.18 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 20.24
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.702→44.681 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: -17.1898 Å / Origin y: -22.937 Å / Origin z: 1.1063 Å
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Refinement TLS group | Selection details: all |