+Open data
-Basic information
Entry | Database: PDB / ID: 1ani | ||||||
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Title | ALKALINE PHOSPHATASE (D153H, K328H) | ||||||
Components | ALKALINE PHOSPHATASE | ||||||
Keywords | ALKALINE PHOSPHATASE / HYDROLASE (PHOSPHORIC MONOESTER) / TRANSFERASE (PHOSPHO / ALCOHOL ACCEPTOR) | ||||||
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 / Resolution: 2.5 Å | ||||||
Authors | Murphy, J.E. / Tibbitts, T.T. / Kantrowitz, E.R. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1995 Title: Mutations at positions 153 and 328 in Escherichia coli alkaline phosphatase provide insight towards the structure and function of mammalian and yeast alkaline phosphatases. Authors: Murphy, J.E. / Tibbitts, T.T. / Kantrowitz, E.R. #1: Journal: Biochemistry / Year: 1993 Title: Magnesium in the Active Site of Escherichia Coli Alkaline Phosphatase is Important for Both Structural Stabilization and Catalysis Authors: Janeway, C.M.L. / Xu, X. / Murphy, J.E. / Chaidaroglou, A. / Kantrowitz, E.R. #2: Journal: J.Biol.Chem. / Year: 1993 Title: Conversion of a Magnesium Binding Site Into a Zinc Binding Site by a Single Amino Acid Substitution in Escherichia Coli Alkaline Phosphatase Authors: Murphy, J.E. / Xu, X. / Kantrowitz, E.R. #3: Journal: J.Mol.Biol. / Year: 1991 Title: Reaction Mechanism of Alkaline Phosphatase Based on Crystal Structures. Two Metal Ion Catalysis 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 | 1ani.cif.gz | 174.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ani.ent.gz | 143.8 KB | Display | PDB format |
PDBx/mmJSON format | 1ani.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/an/1ani ftp://data.pdbj.org/pub/pdb/validation_reports/an/1ani | HTTPS FTP |
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-Related 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: 46799.086 Da / Num. of mol.: 2 / Mutation: D153H, K328H Source method: isolated from a genetically manipulated source Details: 65% SATURATING (NH4)2SO4, 100 MM TRIS, 10 MM MGCL2, 10 MM ZNCL2, 2 MM NAH2PO4 AT PH 7.5 Source: (gene. exp.) Escherichia coli (E. coli) / Strain: EK1481 / Gene: PHOA / Plasmid: PEK190 / Gene (production host): PHOA / Production host: Escherichia coli (E. coli) / Strain (production host): SM547 / References: UniProt: P00634, alkaline phosphatase #2: Chemical | ChemComp-ZN / #3: Chemical | ChemComp-PO4 / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.32 Å3/Da / Density % sol: 62.91 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 / Details: pH 7.5 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 9.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 Å |
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Detector | Type: SAN DIEGO MULTIWIRE / Detector: AREA DETECTOR / Date: Oct 28, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→8 Å / Num. obs: 39775 / % possible obs: 91 % / Observed criterion σ(I): 3 / Redundancy: 3 % / Rmerge(I) obs: 0.072 |
Reflection | *PLUS Num. measured all: 118201 / Rmerge(I) obs: 0.072 |
-Processing
Software |
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Refinement | Resolution: 2.5→8 Å / σ(F): 2
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Refine analyze | Luzzati coordinate error obs: 0.25 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor Rfree: 0.233 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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