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- PDB-1alh: KINETICS AND CRYSTAL STRUCTURE OF A MUTANT E. COLI ALKALINE PHOSP... -
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Open data
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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 | ||||||
![]() | ALKALINE PHOSPHATASE | ||||||
![]() | HYDROLASE (PHOSPHORIC MONOESTER) | ||||||
Function / homology | ![]() 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 | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Tibbitts, T.T. / Xu, X. / Kantrowitz, E.R. | ||||||
![]() | ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 219.8 KB | Display | ![]() |
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PDB format | ![]() | 176.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 449.8 KB | Display | ![]() |
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Full document | ![]() | 461.9 KB | Display | |
Data in XML | ![]() | 35.6 KB | Display | |
Data in CIF | ![]() | 49.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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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.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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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 % |
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Processing
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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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