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Yorodumi- PDB-2iyy: Shikimate kinase from Mycobacterium tuberculosis in complex with ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2iyy | ||||||
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Title | Shikimate kinase from Mycobacterium tuberculosis in complex with shikimate-3-phosphate and SO4 | ||||||
Components | SHIKIMATE KINASE | ||||||
Keywords | TRANSFERASE / AROMATIC AMINO ACID BIOSYNTHESIS / KINASE / MAGNESIUM / P-LOOP KINASE / METAL-BINDING / SHIKIMATE KINASE / SHIKIMATE PATHWAY / NUCLEOTIDE-BINDING / AMINO-ACID BIOSYNTHESIS / ATP-BINDING | ||||||
Function / homology | Function and homology information shikimate kinase / shikimate metabolic process / Chorismate via Shikimate Pathway / shikimate kinase activity / chorismate biosynthetic process / aromatic amino acid family biosynthetic process / amino acid biosynthetic process / phosphorylation / magnesium ion binding / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | MYCOBACTERIUM TUBERCULOSIS (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.62 Å | ||||||
Authors | Hartmann, M.D. / Bourenkov, G.P. / Oberschall, A. / Strizhov, N. / Bartunik, H.D. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2006 Title: Mechanism of Phosphoryl Transfer Catalyzed by Shikimate Kinase from Mycobacterium Tuberculosis. Authors: Hartmann, M.D. / Bourenkov, G.P. / Oberschall, A. / Strizhov, N. / Bartunik, H.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2iyy.cif.gz | 62 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2iyy.ent.gz | 45.3 KB | Display | PDB format |
PDBx/mmJSON format | 2iyy.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/iy/2iyy ftp://data.pdbj.org/pub/pdb/validation_reports/iy/2iyy | HTTPS FTP |
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-Related structure data
Related structure data | 2iyqC 2iyrC 2iysC 2iytC 2iyuC 2iyvC 2iywC 2iyxSC 2iyzC C: citing same article (ref.) S: Starting model for refinement |
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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 on special symmetry positions |
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-Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 19683.506 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) MYCOBACTERIUM TUBERCULOSIS (bacteria) / Strain: H37RV / Production host: ESCHERICHIA COLI (E. coli) References: UniProt: P0A4Z2, UniProt: P9WPY3*PLUS, shikimate kinase |
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-Non-polymers , 6 types, 256 molecules
#2: Chemical | ChemComp-S3P / | ||||||||
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#3: Chemical | ChemComp-SO4 / #4: Chemical | ChemComp-PO4 / | #5: Chemical | #6: Chemical | #7: Water | ChemComp-HOH / | |
-Details
Sequence details | C-TERMINAL HIS-TAG |
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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: 2.5 Å3/Da / Density % sol: 50.9 % |
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Crystal grow | pH: 8 / Details: 200MM MGSO4, 20%(W/V) PEG 3350, pH 8.00 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: MPG/DESY, HAMBURG / Beamline: BW6 / Wavelength: 1.05 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Aug 10, 2005 / Details: MIRRORS |
Radiation | Monochromator: SI111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.05 Å / Relative weight: 1 |
Reflection | Resolution: 1.62→19.16 Å / Num. obs: 25604 / % possible obs: 93.8 % / Redundancy: 2.31 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 5.7 |
Reflection shell | Resolution: 1.62→1.66 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.95 / Mean I/σ(I) obs: 1.4 / % possible all: 92.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2IYX Resolution: 1.62→19.16 Å / Cor.coef. Fo:Fc: 0.971 / Cor.coef. Fo:Fc free: 0.949 / SU B: 2.33 / SU ML: 0.08 / Cross valid method: THROUGHOUT / ESU R: 0.098 / ESU R Free: 0.109 / 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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 24.6 Å2
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Refinement step | Cycle: LAST / Resolution: 1.62→19.16 Å
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Refine LS restraints |
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