+Open data
-Basic information
Entry | Database: PDB / ID: 1anj | |||||||||
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Title | ALKALINE PHOSPHATASE (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: 2.3 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: Biochemistry / Year: 1991 Title: A Water-Mediated Salt Link in the Catalytic Site of Escherichia Coli Alkaline Phosphatase May Influence Activity Authors: 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 | 1anj.cif.gz | 175.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1anj.ent.gz | 144.9 KB | Display | PDB format |
PDBx/mmJSON format | 1anj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/an/1anj ftp://data.pdbj.org/pub/pdb/validation_reports/an/1anj | 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: 46776.027 Da / Num. of mol.: 2 / Mutation: 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: EK1410 / Plasmid: PEK145 / 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: 3.33 Å3/Da / Density % sol: 63.12 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 / Details: pH 7.5 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 9.5 / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||||
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: Jul 27, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→8 Å / Num. obs: 55520 / % possible obs: 99 % / Observed criterion σ(I): 3 / Redundancy: 3.9 % / Rmerge(I) obs: 0.08 |
Reflection | *PLUS Num. measured all: 214198 / Rmerge(I) obs: 0.08 |
-Processing
Software |
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Refinement | Resolution: 2.3→8 Å / σ(F): 2
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Refine analyze | Luzzati coordinate error obs: 0.27 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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