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Open data
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Basic information
Entry | Database: PDB / ID: 5z09 | ||||||
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Title | ST0452(Y97N)-UTP binding form | ||||||
![]() | Dual sugar-1-phosphate nucleotidylyltransferase | ||||||
![]() | SUGAR BINDING PROTEIN / UTP binding | ||||||
Function / homology | ![]() galactosamine-1-phosphate N-acetyltransferase / UDP-N-acetylgalactosamine diphosphorylase / UDP-N-acetylgalactosamine diphosphorylase activity / UTP-glucose-1-phosphate uridylyltransferase / UTP:glucose-1-phosphate uridylyltransferase activity / glucosamine-1-phosphate N-acetyltransferase / glucosamine-1-phosphate N-acetyltransferase activity / glucose-1-phosphate thymidylyltransferase / glucose-1-phosphate thymidylyltransferase activity / UDP-N-acetylglucosamine diphosphorylase ...galactosamine-1-phosphate N-acetyltransferase / UDP-N-acetylgalactosamine diphosphorylase / UDP-N-acetylgalactosamine diphosphorylase activity / UTP-glucose-1-phosphate uridylyltransferase / UTP:glucose-1-phosphate uridylyltransferase activity / glucosamine-1-phosphate N-acetyltransferase / glucosamine-1-phosphate N-acetyltransferase activity / glucose-1-phosphate thymidylyltransferase / glucose-1-phosphate thymidylyltransferase activity / UDP-N-acetylglucosamine diphosphorylase / UDP-N-acetylglucosamine diphosphorylase activity / UDP-N-acetylglucosamine biosynthetic process / nucleotide binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Honda, Y. / Nakano, S. / Ito, S. / Dadashipour, M. / Zhang, Z. / Kawarabayasi, Y. | ||||||
![]() | ![]() Title: Improvement of ST0452N-Acetylglucosamine-1-Phosphate Uridyltransferase Activity by the Cooperative Effect of Two Single Mutations Identified through Structure-Based Protein Engineering Authors: Honda, Y. / Nakano, S. / Ito, S. / Dadashipour, M. / Zhang, Z. / Kawarabayasi, Y. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 458.5 KB | Display | ![]() |
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PDB format | ![]() | 373.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.8 MB | Display | ![]() |
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Full document | ![]() | 1.8 MB | Display | |
Data in XML | ![]() | 79.1 KB | Display | |
Data in CIF | ![]() | 104.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5z0aC ![]() 2ggoS 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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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: _ / Beg auth comp-ID: MET / Beg label comp-ID: MET / End auth comp-ID: VAL / End label comp-ID: VAL / Refine code: _ / Auth seq-ID: 1 - 401 / Label seq-ID: 1 - 401
NCS ensembles :
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Components
#1: Protein | Mass: 45595.430 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: DSM 16993 / JCM 10545 / NBRC 100140 / 7 / Gene: ST0452, STK_04520 / Production host: ![]() ![]() References: UniProt: Q975F9, Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases #2: Chemical | ChemComp-UTP / |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52.7 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop Details: 20%(w/v) PEG3350, 0.2M potassium citrate tribasic monohydrate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Dec 5, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→153 Å / Num. obs: 61139 / % possible obs: 99 % / Redundancy: 6.8 % / Rmerge(I) obs: 0.092 / Net I/σ(I): 16.6 |
Reflection shell | Resolution: 2.9→2.98 Å / Rmerge(I) obs: 0.513 / Num. unique obs: 3018 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2GGO Resolution: 2.91→152.76 Å / Cor.coef. Fo:Fc: 0.932 / Cor.coef. Fo:Fc free: 0.899 / SU B: 19.996 / SU ML: 0.365 / Cross valid method: THROUGHOUT / ESU R Free: 0.445 / 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: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 83.069 Å2
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Refinement step | Cycle: 1 / Resolution: 2.91→152.76 Å
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Refine LS restraints |
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