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Yorodumi- PDB-5ydb: Crystal structure of the complex of type II dehydroquinate dehydr... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5ydb | ||||||
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Title | Crystal structure of the complex of type II dehydroquinate dehydratase from Acinetobacter baumannii with dehydroquinic acid at 1.76 Angstrom resolution | ||||||
Components | 3-dehydroquinate dehydratase | ||||||
Keywords | LYASE | ||||||
Function / homology | Function and homology information quinate catabolic process / 3-dehydroquinate dehydratase / 3-dehydroquinate dehydratase activity / chorismate biosynthetic process / aromatic amino acid family biosynthetic process / amino acid biosynthetic process Similarity search - Function | ||||||
Biological species | Acinetobacter baumannii (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.76 Å | ||||||
Authors | Iqbal, N. / Kaur, P. / Sharma, S. / Singh, T.P. | ||||||
Citation | Journal: To Be Published Title: Crystal structure of the complex of type II dehydroquinate dehydratase from Acinetobacter baumannii with dehydroquinic acid at 1.76 Angstrom resolution Authors: Iqbal, N. / Kaur, P. / Sharma, S. / Singh, T.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5ydb.cif.gz | 236.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5ydb.ent.gz | 191.9 KB | Display | PDB format |
PDBx/mmJSON format | 5ydb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5ydb_validation.pdf.gz | 478.1 KB | Display | wwPDB validaton report |
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Full document | 5ydb_full_validation.pdf.gz | 492.2 KB | Display | |
Data in XML | 5ydb_validation.xml.gz | 26.6 KB | Display | |
Data in CIF | 5ydb_validation.cif.gz | 36.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yd/5ydb ftp://data.pdbj.org/pub/pdb/validation_reports/yd/5ydb | HTTPS FTP |
-Related structure data
Related structure data | 5b6pS 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
#1: Protein | Mass: 16184.426 Da / Num. of mol.: 4 / Fragment: UNP residues 3-150 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377) (bacteria) Strain: ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377 Gene: aroQ, A1S_2009 / Production host: Escherichia coli (E. coli) / References: UniProt: A3M692, 3-dehydroquinate dehydratase #2: Chemical | ChemComp-NA / #3: Chemical | ChemComp-DQA / #4: 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: 2.33 Å3/Da / Density % sol: 47.24 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 0.05M Cadmium sulfate hydrate, 0.1M HEPES, PH 7.5, IM Sodium acetate trihydrate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: MASSIF-3 / Wavelength: 0.97 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jul 5, 2017 / Details: MIRROR |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Resolution: 1.76→69.56 Å / Num. obs: 56929 / % possible obs: 98.3 % / Redundancy: 2.8 % / Net I/σ(I): 8.2 |
Reflection shell | Resolution: 1.76→1.82 Å / Redundancy: 2.8 % / Mean I/σ(I) obs: 0.7 / % possible all: 98.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5B6P Resolution: 1.76→69.56 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.94 / SU B: 10.02 / SU ML: 0.141 / Cross valid method: THROUGHOUT / ESU R: 0.132 / ESU R Free: 0.133 / 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: 48.171 Å2
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Refinement step | Cycle: 1 / Resolution: 1.76→69.56 Å
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Refine LS restraints |
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