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- PDB-3qqs: Anthranilate phosphoribosyltransferase (TRPD) from Mycobacterium ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3qqs | ||||||
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Title | Anthranilate phosphoribosyltransferase (TRPD) from Mycobacterium tuberculosis (complex with inhibitor ACS172) | ||||||
![]() | Anthranilate phosphoribosyltransferase | ||||||
![]() | Transferase/Transferase Inhibitor / Anthranilate Phosphoribosyltransferase / Anthranilic Acids / Magnesium / Tryptophan / Magnesium binding / Phosphoribosyl pyrophosphate / Transferase-Transferase Inhibitor complex / Structural Genomics / TB Structural Genomics Consortium / TBSGC | ||||||
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. / Short, F.L. / Lott, J.S. / TB Structural Genomics Consortium (TBSGC) | ||||||
![]() | ![]() Title: The Substrate Capture Mechanism of Mycobacterium tuberculosis Anthranilate Phosphoribosyltransferase Provides a Mode for Inhibition. Authors: Castell, A. / Short, F.L. / Evans, G.L. / Cookson, T.V. / Bulloch, E.M. / Joseph, D.D. / Lee, C.E. / Parker, E.J. / Baker, E.N. / Lott, J.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 269.5 KB | Display | ![]() |
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PDB format | ![]() | 217.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 3.7 MB | Display | ![]() |
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Full document | ![]() | 3.7 MB | Display | |
Data in XML | ![]() | 56.7 KB | Display | |
Data in CIF | ![]() | 79.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3qr9C ![]() 3qs8C ![]() 3r6cC ![]() 3r88C ![]() 3twpC ![]() 3uu1C ![]() 1zvwS S: Starting model for refinement C: citing same article ( |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Components
-Protein / Sugars , 2 types, 7 molecules ABCD![](data/chem/img/PRP.gif)
![](data/chem/img/PRP.gif)
#1: Protein | Mass: 38717.688 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P66992, UniProt: P9WFX5*PLUS, anthranilate phosphoribosyltransferase #2: Sugar | |
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-Non-polymers , 4 types, 614 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/17C.gif)
![](data/chem/img/DPO.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/17C.gif)
![](data/chem/img/DPO.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-MG / #4: Chemical | ChemComp-17C / #5: Chemical | ChemComp-DPO / | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.28 Å3/Da / Density % sol: 45.95 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 0.2 M cacodylate, 7% PEG6000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ![]() |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Jun 4, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54179 Å / Relative weight: 1 |
Reflection | Resolution: 1.97→94.9 Å / Num. obs: 97403 / % possible obs: 99.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 3.7 % / Rmerge(I) obs: 0.091 / Rsym value: 0.106 |
Reflection shell | Resolution: 1.97→2.08 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.72 / Mean I/σ(I) obs: 2 / Rsym value: 0.84 / % possible all: 97.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 1zvw Resolution: 1.97→88.75 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.922 / Occupancy max: 1 / Occupancy min: 0.4 / SU B: 4.972 / SU ML: 0.14 / SU R Cruickshank DPI: 0.1949 / Cross valid method: THROUGHOUT / ESU R: 0.202 / ESU R Free: 0.177 / Stereochemistry target values: MAXIMUM LIKELIHOOD / 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: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 26.272 Å2
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Refinement step | Cycle: LAST / Resolution: 1.97→88.75 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.97→2.021 Å / Total num. of bins used: 20
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