+Open data
-Basic information
Entry | Database: PDB / ID: 2vef | ||||||
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Title | Dihydropteroate synthase from Streptococcus pneumoniae | ||||||
Components | DIHYDROPTEROATE SYNTHASE | ||||||
Keywords | TRANSFERASE / ANTIBIOTIC RESISTANCE / FOLATE BIOSYNTHESIS | ||||||
Function / homology | Function and homology information dihydropteroate synthase / dihydropteroate synthase activity / folic acid biosynthetic process / tetrahydrofolate biosynthetic process / response to antibiotic / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | STREPTOCOCCUS PNEUMONIAE (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.8 Å | ||||||
Authors | Derrick, J.P. / Levy, C. | ||||||
Citation | Journal: Biochem.J. / Year: 2008 Title: Dihydropteroate Synthase from Streptococcus Pneumoniae: Structure, Ligand Recognition and Mechanism of Sulfonamide Resistance. Authors: Levy, C. / Minnis, D. / Derrick, J.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2vef.cif.gz | 126.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2vef.ent.gz | 100.5 KB | Display | PDB format |
PDBx/mmJSON format | 2vef.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2vef_validation.pdf.gz | 448.2 KB | Display | wwPDB validaton report |
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Full document | 2vef_full_validation.pdf.gz | 452.5 KB | Display | |
Data in XML | 2vef_validation.xml.gz | 26.5 KB | Display | |
Data in CIF | 2vef_validation.cif.gz | 40.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ve/2vef ftp://data.pdbj.org/pub/pdb/validation_reports/ve/2vef | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.97, -0.194, 0.148), Vector: |
-Components
#1: Protein | Mass: 34457.195 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) STREPTOCOCCUS PNEUMONIAE (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P59655, dihydropteroate synthase #2: Chemical | ChemComp-PO4 / | #3: Water | ChemComp-HOH / | Sequence details | DIPEPTIDE 'IE' REMOVED FROM THE SEQUENCE AT POSITION 65, AS THIS CORRESPONDS TO THE SULPHONAMIDE ...DIPEPTIDE 'IE' REMOVED FROM THE SEQUENCE AT POSITION 65, AS THIS CORRESPOND | |
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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: 2.2 Å3/Da / Density % sol: 44.1 % / Description: NONE |
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Crystal grow | Details: 0.2 M AMMONIUM IODIDE, 20% (W/V) POLYETHYLENE GLYCOL 3,350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SRS / Beamline: PX14.1 / Wavelength: 1.488 |
Detector | Type: ADSC CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.488 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→55 Å / Num. obs: 65291 / % possible obs: 99 % / Observed criterion σ(I): 4 / Redundancy: 3.43 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 12.7 |
Reflection shell | Resolution: 1.8→1.9 Å / Redundancy: 2.89 % / Rmerge(I) obs: 0.21 / Mean I/σ(I) obs: 4.5 / % possible all: 93.9 |
-Processing
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Refinement | Method to determine structure: SAD Starting model: NONE Resolution: 1.8→45.18 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.928 / SU B: 5.816 / SU ML: 0.098 / TLS residual ADP flag: UNVERIFIED / Cross valid method: THROUGHOUT / ESU R: 0.139 / ESU R Free: 0.136 / 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: 14 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→45.18 Å
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