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- PDB-1ajc: THREE-DIMENSIONAL STRUCTURE OF THE D153G MUTANT OF E. COLI ALKALI... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ajc | ||||||
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Title | THREE-DIMENSIONAL STRUCTURE OF THE D153G MUTANT OF E. COLI ALKALINE PHOSPHATASE: A MUTANT WITH WEAKER MAGNESIUM BINDING AND INCREASED CATALYTIC ACTIVITY | ||||||
![]() | ALKALINE PHOSPHATASE | ||||||
![]() | NON SPECIFIC MONO-ESTERASE | ||||||
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 | ![]() | ||||||
![]() | Dealwis, C.G. / Chen, L. / Abad-Zapatero, C. | ||||||
![]() | ![]() Title: Crystallographic analysis of reversible metal binding observed in a mutant (Asp153-->Gly) of Escherichia coli alkaline phosphatase. Authors: Dealwis, C.G. / Brennan, C. / Christianson, K. / Mandecki, W. / Abad-Zapatero, C. #1: ![]() Title: Crystallographic Analysis of Reversible Metal Binding Observed in a Mutant (Asp 153--> Gly) of E. Coli Alkaline Phosphatase Authors: Dealwis, C. / Brennan, C. / Christianson, K. / Mandecki, W. / Abad-Zapatero, A. #2: ![]() Title: 3-D Structure of the (Asp 101-->Ser) of E.Coli Alkaline Phosphatase with Higher Catalytic Activity Authors: Chen, L. / Neidhart, D. / Kohlbrenner, M. / Mandecki, W. / Bell, S. / Sowadski, J. / Abad-Zapatero, C. | ||||||
History |
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Remark 700 | SHEET SHEET DETERMINATION METHOD: KABSCH & SANDER; SHEET_ID: S1A; SAME AS 1ALK. SHEET_ID: S2A; SAME ...SHEET SHEET DETERMINATION METHOD: KABSCH & SANDER; SHEET_ID: S1A; SAME AS 1ALK. SHEET_ID: S2A; SAME AS 1ALK. SHEET_ID: S1B; SAME AS 1ALK. SHEET_ID: S2B; SAME AS 1ALK. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 165.6 KB | Display | ![]() |
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PDB format | ![]() | 137.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 376 KB | Display | ![]() |
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Full document | ![]() | 394.6 KB | Display | |
Data in XML | ![]() | 19.8 KB | Display | |
Data in CIF | ![]() | 29.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 47037.348 Da / Num. of mol.: 2 / Mutation: D153G Source method: isolated from a genetically manipulated source Details: MUTANT WITH 4-FOLD INCREASED ACTIVITY AND WEAKER MG BINDING Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-ZN / #3: Chemical | #4: Water | ChemComp-HOH / | Source details | FOR MORE INFORMATIO | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.31 Å3/Da / Density % sol: 62.78 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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 |
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Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Jan 6, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 40175 / % possible obs: 77 % / Observed criterion σ(I): 0 / Redundancy: 1.66 % / Rmerge(I) obs: 0.103 |
Reflection | *PLUS Highest resolution: 2.8 Å / Num. obs: 25993 / % possible obs: 82.2 % / Rmerge(I) obs: 0.103 |
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Processing
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Refinement | Resolution: 2.5→6 Å / σ(F): 0 /
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Displacement parameters | Biso mean: 11 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→6 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.195 / Highest resolution: 2.8 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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