+Open data
-Basic information
Entry | Database: PDB / ID: 6b5k | ||||||
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Title | Mycobacterium tuberculosis RmlA in complex with Mg/dTTP | ||||||
Components | Glucose-1-phosphate thymidylyltransferase | ||||||
Keywords | TRANSFERASE / nucleotidyltransferase / substrate / sugar-modifying | ||||||
Function / homology | Function and homology information dTTP metabolic process / glucose-1-phosphate thymidylyltransferase / glucose-1-phosphate thymidylyltransferase activity / dTDP-rhamnose biosynthetic process / extracellular polysaccharide biosynthetic process / peptidoglycan-based cell wall / glucose metabolic process / magnesium ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | Mycobacterium tuberculosis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.6 Å | ||||||
Authors | Brown, H.A. / Holden, H.A. | ||||||
Funding support | United States, 1items
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Citation | Journal: Protein Sci. / Year: 2018 Title: The structure of glucose-1-phosphate thymidylyltransferase from Mycobacterium tuberculosis reveals the location of an essential magnesium ion in the RmlA-type enzymes. Authors: Brown, H.A. / Thoden, J.B. / Tipton, P.A. / Holden, H.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6b5k.cif.gz | 133.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6b5k.ent.gz | 100.9 KB | Display | PDB format |
PDBx/mmJSON format | 6b5k.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b5/6b5k ftp://data.pdbj.org/pub/pdb/validation_reports/b5/6b5k | HTTPS FTP |
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-Related structure data
Related structure data | 6b5eC 1h5sS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 32592.039 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (bacteria) Strain: ATCC 25618 / H37Rv / Gene: rmlA, rfbA, Rv0334 / Production host: Escherichia coli BL21(DE3) (bacteria) References: UniProt: P9WH13, glucose-1-phosphate thymidylyltransferase |
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-Non-polymers , 5 types, 358 molecules
#2: Chemical | #3: Chemical | ChemComp-MG / #4: Chemical | #5: Chemical | ChemComp-EDO / | #6: 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: 2.97 Å3/Da / Density % sol: 58.53 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 18 - 22% poly(ethylene glycol) 8000 and 100 mM MOPS |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 19-BM / Wavelength: 0.9794 Å |
Detector | Type: ADSC QUANTUM 210r / Detector: CCD / Date: Jun 24, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9794 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→50 Å / Num. obs: 89386 / % possible obs: 98.5 % / Redundancy: 5.9 % / Rsym value: 0.049 / Net I/σ(I): 55.7 |
Reflection shell | Resolution: 1.6→1.66 Å / Redundancy: 3.7 % / Mean I/σ(I) obs: 5.9 / Num. unique obs: 8778 / Rsym value: 0.198 / % possible all: 97 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1H5S Resolution: 1.6→50 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.941 / SU B: 1.709 / SU ML: 0.06 / Cross valid method: THROUGHOUT / ESU R: 0.085 / ESU R Free: 0.087 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 31.691 Å2
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Refinement step | Cycle: 1 / Resolution: 1.6→50 Å
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Refine LS restraints |
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