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Yorodumi- PDB-1alh: KINETICS AND CRYSTAL STRUCTURE OF A MUTANT E. COLI ALKALINE PHOSP... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1alh | ||||||
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Title | KINETICS AND CRYSTAL STRUCTURE OF A MUTANT E. COLI ALKALINE PHOSPHATASE (ASP-369-->ASN): A MECHANISM INVOLVING ONE ZINC PER ACTIVE SITE | ||||||
Components | ALKALINE PHOSPHATASE | ||||||
Keywords | HYDROLASE (PHOSPHORIC MONOESTER) | ||||||
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 | Tibbitts, T.T. / Xu, X. / Kantrowitz, E.R. | ||||||
Citation | Journal: Protein Sci. / Year: 1994 Title: Kinetics and crystal structure of a mutant Escherichia coli alkaline phosphatase (Asp-369-->Asn): a mechanism involving one zinc per active site. Authors: Tibbitts, T.T. / Xu, X. / 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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1alh.cif.gz | 215.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1alh.ent.gz | 181.3 KB | Display | PDB format |
PDBx/mmJSON format | 1alh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/al/1alh ftp://data.pdbj.org/pub/pdb/validation_reports/al/1alh | 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
#1: Protein | Mass: 46767.062 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Cell line: SM547 / Gene: PHOA / Plasmid: PEK209 / Gene (production host): PHOA / Production host: Escherichia coli (E. coli) / Strain (production host): SM547 / References: UniProt: P00634, alkaline phosphatase #2: Chemical | #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: 62.89 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 42809 / % possible obs: 98.4 % / Observed criterion σ(I): 3 |
Reflection | *PLUS Num. all: 43509 / Redundancy: 7.5 % |
-Processing
Software |
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Refinement | Resolution: 2.5→8 Å / σ(F): 2 Details: THE DENSITY IS VERY WEAK OR ABSENT FOR RESIDUES 1, 2, 3, 293, AND 408. THEREFORE RESIDUES 1 - 3 ARE OMITTED, AND THE ATOMIC COORDINATES LISTED FOR RESIDUES 293 AND 408 HAVE A LARGE UNCERTAINTY.
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Displacement parameters | Biso mean: 22 Å2 | ||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints | *PLUS
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