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- PDB-4owm: Anthranilate phosphoribosyl transferase from Mycobacterium tuberc... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4owm | ||||||
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Title | Anthranilate phosphoribosyl transferase from Mycobacterium tuberculosis in complex with 3-fluoroanthranilate, PRPP and Magnesium | ||||||
![]() | Anthranilate phosphoribosyltransferase | ||||||
![]() | TRANSFERASE / Anthranilic Acids / Magnesium / Tryptophan / Inhibitor | ||||||
Function / homology | ![]() anthranilate phosphoribosyltransferase / anthranilate phosphoribosyltransferase activity / tryptophan biosynthetic process / magnesium ion binding / extracellular region / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Castell, A. / Cookson, T.V.M. / Short, F.L. / Lott, J.S. | ||||||
![]() | ![]() Title: Alternative substrates reveal catalytic cycle and key binding events in the reaction catalysed by anthranilate phosphoribosyltransferase from Mycobacterium tuberculosis. Authors: Cookson, T.V. / Castell, A. / Bulloch, E.M. / Evans, G.L. / Short, F.L. / Baker, E.N. / Lott, J.S. / Parker, E.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 270.4 KB | Display | ![]() |
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PDB format | ![]() | 218 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 30.6 KB | Display | |
Data in CIF | ![]() | 45.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4n5vC ![]() 4n8qC ![]() 4n93C ![]() 4ownC ![]() 4owoC ![]() 4owqC ![]() 4owsC ![]() 4owuC ![]() 4owvC 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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Components
-Protein / Sugars , 2 types, 4 molecules AB![](data/chem/img/PRP.gif)
![](data/chem/img/PRP.gif)
#1: Protein | Mass: 38848.883 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P66992, UniProt: P9WFX5*PLUS, anthranilate phosphoribosyltransferase #3: Sugar | |
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-Non-polymers , 5 types, 461 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/3F0.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/IMD.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/3F0.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/IMD.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-MG / #4: Chemical | #5: Chemical | ChemComp-GOL / | #6: Chemical | ChemComp-IMD / | #7: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.06 Å3/Da / Density % sol: 59.85 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / Details: imidazole/malate, PEG 4000 |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 13, 2010 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.95369 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 1.99→120.892 Å / Num. all: 52873 / Num. obs: 52873 / % possible obs: 86.9 % / Redundancy: 4.6 % / Rpim(I) all: 0.046 / Rrim(I) all: 0.105 / Rsym value: 0.085 / Net I/av σ(I): 7.8 / Net I/σ(I): 12.2 / Num. measured all: 245631 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1 / Rejects: _
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Processing
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Refinement | Resolution: 1.99→73.21 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.937 / SU B: 6.072 / SU ML: 0.087 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.162 / ESU R Free: 0.151 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : RESIDUAL ONLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 66.46 Å2 / Biso mean: 22.213 Å2 / Biso min: 11.11 Å2
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Refinement step | Cycle: final / Resolution: 1.99→73.21 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.993→2.045 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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