+Open data
-Basic information
Entry | Database: PDB / ID: 1ali | ||||||
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Title | ALKALINE PHOSPHATASE MUTANT (H412N) | ||||||
Components | ALKALINE PHOSPHATASE | ||||||
Keywords | 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 / 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: 2.2 Å | ||||||
Authors | Ma, L. / Tibbitts, T.T. / Kantrowitz, E.R. | ||||||
Citation | Journal: Protein Sci. / Year: 1995 Title: Escherichia coli alkaline phosphatase: X-ray structural studies of a mutant enzyme (His-412-->Asn) at one of the catalytically important zinc binding sites. Authors: Ma, L. / Tibbitts, T.T. / Kantrowitz, E.R. #1: 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. #2: Journal: J.Biol.Chem. / Year: 1994 Title: Mutations at Histidine 412 Alter Zinc Binding and Eliminate Transferase Activity in Escherichia Coli Alkaline Phosphatase Authors: Ma, L. / Kantrowitz, E.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ali.cif.gz | 172.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ali.ent.gz | 143.6 KB | Display | PDB format |
PDBx/mmJSON format | 1ali.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ali_validation.pdf.gz | 389.4 KB | Display | wwPDB validaton report |
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Full document | 1ali_full_validation.pdf.gz | 400.2 KB | Display | |
Data in XML | 1ali_validation.xml.gz | 19.2 KB | Display | |
Data in CIF | 1ali_validation.cif.gz | 30.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/al/1ali ftp://data.pdbj.org/pub/pdb/validation_reports/al/1ali | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | THERE IS A DIMER (IDENTICAL CHAINS OF 449 RESIDUES) PER ASYMMETRIC UNIT. THESE SUBUNITS ARE DESIGNATED "A" AND "B". THE FIRST THREE RESIDUES WERE DELETED DURING THE REFINEMENT. |
-Components
#1: Protein | Mass: 47070.355 Da / Num. of mol.: 2 / Mutation: H412N Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: EK1498 / Gene: PHOA / Plasmid: PEK202 / Gene (production host): PHOA / 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 |
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-Sample preparation
Crystal | Density Matthews: 3.31 Å3/Da / Density % sol: 62.88 % | ||||||||||||||||||||||||
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Crystal grow | Details: THE STRUCTURE IS OF A MUTANT ALKALINE PHOSPHATE (H412N) IN WHICH HIS 412 IS REPLACED BY ASN, DETERMINED WITH CRYSTALS SOAKED IN STABILIZATION BUFFER CONTAINING 10 MM ZINC CHLORIDE. THERE ARE ...Details: THE STRUCTURE IS OF A MUTANT ALKALINE PHOSPHATE (H412N) IN WHICH HIS 412 IS REPLACED BY ASN, DETERMINED WITH CRYSTALS SOAKED IN STABILIZATION BUFFER CONTAINING 10 MM ZINC CHLORIDE. THERE ARE TWO ZINCS AND ONE MAGNESIUM COMPLEXED WITH AN INORGANIC PHOSPHATE BOUND IN EACH OF THE TWO ACTIVE SITES. | ||||||||||||||||||||||||
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: 1.54 |
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Detector | Type: ADSC / Detector: AREA DETECTOR / Date: Jan 23, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→39.3 Å / Num. obs: 63998 / % possible obs: 99.3 % / Observed criterion σ(I): 3 / Redundancy: 3.5 % / Rmerge(I) obs: 0.087 |
Reflection | *PLUS Num. measured all: 224987 / Rmerge(I) obs: 0.087 |
-Processing
Software |
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Refinement | Resolution: 2.2→8 Å / σ(F): 0 /
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Refine analyze | Luzzati coordinate error obs: 0.25 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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