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Yorodumi- PDB-2acw: Crystal Structure of Medicago truncatula UGT71G1 complexed with U... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2acw | ||||||
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Title | Crystal Structure of Medicago truncatula UGT71G1 complexed with UDP-glucose | ||||||
Components | triterpene UDP-glucosyl transferase UGT71G1 | ||||||
Keywords | TRANSFERASE / Glycosyltransferase / UDP-glucose | ||||||
Function / homology | Function and homology information UDP-glucosyltransferase activity / Transferases; Glycosyltransferases; Hexosyltransferases / nucleotide binding Similarity search - Function | ||||||
Biological species | Medicago truncatula (barrel medic) | ||||||
Method | X-RAY DIFFRACTION / FOURIER SYNTHESIS / Resolution: 2.6 Å | ||||||
Authors | Shao, H. / He, X. / Achnine, L. / Blount, J.W. / Dixon, R.A. / Wang, X. | ||||||
Citation | Journal: Plant Cell / Year: 2005 Title: Crystal Structures of a Multifunctional Triterpene/Flavonoid Glycosyltransferase from Medicago truncatula. Authors: Shao, H. / He, X. / Achnine, L. / Blount, J.W. / Dixon, R.A. / Wang, X. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2acw.cif.gz | 188.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2acw.ent.gz | 150.8 KB | Display | PDB format |
PDBx/mmJSON format | 2acw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2acw_validation.pdf.gz | 1 MB | Display | wwPDB validaton report |
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Full document | 2acw_full_validation.pdf.gz | 1 MB | Display | |
Data in XML | 2acw_validation.xml.gz | 37.2 KB | Display | |
Data in CIF | 2acw_validation.cif.gz | 49.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ac/2acw ftp://data.pdbj.org/pub/pdb/validation_reports/ac/2acw | HTTPS FTP |
-Related 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: 51836.578 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Medicago truncatula (barrel medic) / Production host: Escherichia coli (E. coli) References: UniProt: Q5IFH7, Transferases; Glycosyltransferases; Hexosyltransferases #2: Chemical | #3: 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: 2.6 Å3/Da / Density % sol: 47 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: PEG 3350, ammonium acetate, sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH3R / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Apr 8, 2005 |
Radiation | Monochromator: Osmic Confocal MAX-Flux / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→100 Å / Num. all: 29545 / Num. obs: 29545 / % possible obs: 99.8 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Rmerge(I) obs: 0.059 / Net I/σ(I): 12.1 |
Reflection shell | Resolution: 2.6→2.69 Å / Rmerge(I) obs: 0.442 / Mean I/σ(I) obs: 2.3 / Num. unique all: 2936 / % possible all: 99.7 |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS / Resolution: 2.6→99.1 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refine analyze | Luzzati coordinate error obs: 0.32 Å | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→99.1 Å
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Refine LS restraints |
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