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Yorodumi- PDB-1kh4: E. COLI ALKALINE PHOSPHATASE MUTANT (D330N) IN COMPLEX WITH PHOSPHATE -
+Open data
-Basic information
Entry | Database: PDB / ID: 1kh4 | ||||||
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Title | E. COLI ALKALINE PHOSPHATASE MUTANT (D330N) IN COMPLEX WITH PHOSPHATE | ||||||
Components | ALKALINE PHOSPHATASE | ||||||
Keywords | HYDROLASE / ALKALINE PHOSPHATASE | ||||||
Function / homology | Function and homology information oxidoreductase activity, acting on phosphorus or arsenic in donors / alkaline phosphatase / alkaline phosphatase activity / hydrogenase (acceptor) activity / phosphoprotein phosphatase activity / dephosphorylation / protein dephosphorylation / outer membrane-bounded periplasmic space / periplasmic space / magnesium ion binding / zinc ion binding Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Le Du, M.H. / Lamoure, C. / Muller, B.H. / Bulgakov, O.V. / Lajeunesse, E. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2002 Title: Artificial evolution of an enzyme active site: structural studies of three highly active mutants of Escherichia coli alkaline phosphatase. Authors: Le Du, M.H. / Lamoure, C. / Muller, B.H. / Bulgakov, O.V. / Lajeunesse, E. / Menez, A. / Boulain, J.C. #1: Journal: J.Mol.Biol. / Year: 1991 Title: Reaction Mechanism of Alkaline Phosphatase Based on Crystal Structures. Two-Metal Ion Catalysi Authors: Kim, E.E. / Wyckoff, H.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1kh4.cif.gz | 179.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1kh4.ent.gz | 141.7 KB | Display | PDB format |
PDBx/mmJSON format | 1kh4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kh/1kh4 ftp://data.pdbj.org/pub/pdb/validation_reports/kh/1kh4 | HTTPS FTP |
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-Related structure data
Related structure data | 1kh5C 1kh7C 1kh9C 1khjC 1khkC 1khlC 1khnC 1alkS 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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.00713, 0.999974, -0.001354), Vector: |
-Components
#1: Protein | Mass: 47092.426 Da / Num. of mol.: 2 / Mutation: D330N Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: WCC118 / Gene: PHOAD330N / Plasmid: PLIP4.0D153HD330N / Production host: Escherichia coli (E. coli) / References: UniProt: P00634, alkaline phosphatase #2: Chemical | ChemComp-ZN / #3: Chemical | #4: Chemical | #5: 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: 2.85 Å3/Da / Density % sol: 56.81 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8 Details: Ammonium sulfate, magnesium chloride, zinc sulfate, TRIS, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 292 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM02 / Wavelength: 0.98 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: May 1, 1996 |
Radiation | Monochromator: D2AM MIRROR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→20 Å / Num. all: 31594 / Num. obs: 31594 / % possible obs: 73.1 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 0 / Rsym value: 0.062 / Net I/σ(I): 26.9 |
Reflection shell | Resolution: 2.4→2.51 Å / Mean I/σ(I) obs: 4.9 / Rsym value: 0.28 / % possible all: 69 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1ALK Resolution: 2.4→10 Å / Cross valid method: IMPLOR-CYCLING TEST SETS / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2.4→10 Å
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