+Open data
-Basic information
Entry | Database: PDB / ID: 1obw | ||||||
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Title | STRUCTURE OF INORGANIC PYROPHOSPHATASE | ||||||
Components | INORGANIC PYROPHOSPHATASE | ||||||
Keywords | HYDROLASE / MAGNESIUM / METAL BINDING | ||||||
Function / homology | Function and homology information inorganic triphosphate phosphatase activity / inorganic diphosphatase / inorganic diphosphate phosphatase activity / phosphate-containing compound metabolic process / magnesium ion binding / zinc ion binding / membrane / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPL. / Resolution: 1.9 Å | ||||||
Authors | Oganessyan, V.Yu. / Harutyunyan, E.H. / Avaeva, S.M. / Oganessyan, N.N. / Mather, T. / Huber, R. | ||||||
Citation | Journal: Biochemistry / Year: 1997 Title: Crystal structure of holo inorganic pyrophosphatase from Escherichia coli at 1.9 A resolution. Mechanism of hydrolysis. Authors: Harutyunyan, E.H. / Oganessyan, V.Y. / Oganessyan, N.N. / Avaeva, S.M. / Nazarova, T.I. / Vorobyeva, N.N. / Kurilova, S.A. / Huber, R. / Mather, T. #1: Journal: FEBS Lett. / Year: 1994 Title: X-Ray Crystallographic Studies of Recombinant Inorganic Pyrophosphatase from Escherichia Coli Authors: Oganessyan, V.Yu. / Kurilova, S.A. / Vorobyeva, N.N. / Nazarova, T.I. / Popov, A.N. / Lebedev, A.A. / Avaeva, S.M. / Harutyunyan, E.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1obw.cif.gz | 119.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1obw.ent.gz | 93.4 KB | Display | PDB format |
PDBx/mmJSON format | 1obw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ob/1obw ftp://data.pdbj.org/pub/pdb/validation_reports/ob/1obw | HTTPS FTP |
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-Related structure data
Similar structure data |
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-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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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 19585.279 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: JM109 / Plasmid: PUC19 Gene (production host): PYROPHOSPHATASE FROM ESCHERICHIA COLI Production host: Escherichia coli (E. coli) / References: UniProt: P0A7A9, inorganic diphosphatase #2: Chemical | ChemComp-MG / #3: 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: 2.34 Å3/Da / Density % sol: 40 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 / Details: pH 7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 1, 1996 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→20 Å / Num. obs: 41190 / % possible obs: 99.7 % / Observed criterion σ(I): 3 / Redundancy: 6 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 14 |
Reflection shell | Resolution: 1.9→1.95 Å / Redundancy: 3 % / Rmerge(I) obs: 0.244 / Mean I/σ(I) obs: 4 / % possible all: 99.2 |
Reflection | *PLUS % possible obs: 99.6 % / Num. measured all: 360600 / Rmerge(I) obs: 0.077 |
Reflection shell | *PLUS % possible obs: 99.9 % / Rmerge(I) obs: 0.241 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPL. Starting model: REFINED STRUCTURE OF APO-FORM OF THIS ENZYME AT 2.2A. (HARUTYUNYAN ET AL., 1996, CRYSTALLOGRAPHIA(RUS), V.14 ,PP84-96. Resolution: 1.9→15 Å / σ(F): 1 Details: ESTIMATED COORD. ERROR 0.26 ANGSTROMS FINAL RMS COORD. SHIFT 0.002 ANGSTROMS
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Displacement parameters | Biso mean: 34 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.22 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→15 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.176 / Rfactor Rfree: 0.232 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |