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- PDB-8oy0: ATP phosphoribosyltransferase (HisZG ATPPRT) from Acinetobacter b... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8oy0 | ||||||
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Title | ATP phosphoribosyltransferase (HisZG ATPPRT) from Acinetobacter baumanii | ||||||
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![]() | TRANSFERASE / ATPPRT / HisZG / histidine / biosynthesis | ||||||
Function / homology | ![]() ATP phosphoribosyltransferase / ATP phosphoribosyltransferase activity / L-histidine biosynthetic process / glycosyltransferase activity / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Alphey, M.S. / Read, B. / da Silva, R.G. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Crystal Structure, Steady-State, and Pre-Steady-State Kinetics of Acinetobacter baumannii ATP Phosphoribosyltransferase. Authors: Read, B.J. / Cadzow, A.F. / Alphey, M.S. / Mitchell, J.B.O. / da Silva, R.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 892.9 KB | Display | ![]() |
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PDB format | ![]() | 746 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 490.1 KB | Display | ![]() |
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Full document | ![]() | 501 KB | Display | |
Data in XML | ![]() | 76.6 KB | Display | |
Data in CIF | ![]() | 105.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 42960.402 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: The initial Gly remains after cleavage of a purification tag Source: (gene. exp.) ![]() Gene: hisZ / Plasmid: pJexpress414 / Production host: ![]() ![]() #2: Protein | Mass: 25170.256 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: The initial Gly remains after cleavage of a purification tag Source: (gene. exp.) ![]() Gene: hisG / Production host: ![]() ![]() #3: Chemical | ChemComp-GOL / | #4: Chemical | ChemComp-NA / #5: Water | ChemComp-HOH / | Has ligand of interest | N | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.49 Å3/Da / Density % sol: 50.65 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 0.2M sodium nitrate, 0.1M bis-Tris propane pH 8.5, 20% PEG3350 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU SATURN 944+ / Detector: CCD / Date: Jan 27, 2021 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→30.82 Å / Num. obs: 99446 / % possible obs: 95.6 % / Redundancy: 6.4 % / CC1/2: 0.996 / Rmerge(I) obs: 0.124 / Rpim(I) all: 0.051 / Rrim(I) all: 0.135 / Χ2: 0.99 / Net I/σ(I): 9.6 / Num. measured all: 631956 |
Reflection shell | Resolution: 2.4→2.44 Å / % possible obs: 80.6 % / Redundancy: 4.8 % / Rmerge(I) obs: 1.045 / Num. measured all: 19967 / Num. unique obs: 4130 / CC1/2: 0.618 / Rpim(I) all: 0.498 / Rrim(I) all: 1.164 / Χ2: 0.86 / Net I/σ(I) obs: 1.4 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Ion probe radii: 0.7 Å / Shrinkage radii: 0.7 Å / VDW probe radii: 1.1 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 49.623 Å2
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Refinement step | Cycle: 1 / Resolution: 2.4→30.82 Å
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Refine LS restraints |
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