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Open data
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Basic information
Entry | Database: PDB / ID: 1hqa | ||||||
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Title | ALKALINE PHOSPHATASE (H412Q) | ||||||
![]() | ALKALINE PHOSPHATASE | ||||||
![]() | HYDROLASE (ALKALINE PHOSPHATASE) / HYDROLASE / PHOSPHORIC MONOESTER / TRANSFERASE / PHOSPHO / ALCOHOL ACCEPTOR | ||||||
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 | ![]() | ||||||
![]() | Ma, L. / Kantrowitz, E.R. | ||||||
![]() | ![]() Title: Kinetic and X-ray structural studies of a mutant Escherichia coli alkaline phosphatase (His-412-->Gln) at one of the zinc binding sites. Authors: Ma, L. / Kantrowitz, E.R. #1: ![]() 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. #2: ![]() Title: Mutations at Histidine 412 Alter Zinc Binding and Eliminate Transferase Activity in Escherichia Coli Alkaline Phosphatase Authors: Ma, L. / Kantrowitz, E.R. #3: ![]() 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 | ![]() | 175.9 KB | Display | ![]() |
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PDB format | ![]() | 145.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 374.9 KB | Display | ![]() |
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Full document | ![]() | 386.7 KB | Display | |
Data in XML | ![]() | 18.4 KB | Display | |
Data in CIF | ![]() | 30.7 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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Unit cell |
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Components
#1: Protein | Mass: 47084.383 Da / Num. of mol.: 2 / Mutation: H412Q Source method: isolated from a genetically manipulated source Details: CRYSTALLIZED FROM 55% SATURATING (NH4)2SO4, 100 MM TRIS, 10 MM MGCL2 10 MM ZNCL2, 2 MM NAH2PO4, PH 7.5 Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-ZN / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.32 Å3/Da / Density % sol: 62.91 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 / Details: pH 7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 9.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 275 K |
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Diffraction source | Source: ![]() |
Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR / Date: Aug 10, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→40.9 Å / Num. obs: 58551 / % possible obs: 98 % / Observed criterion σ(I): 3 / Redundancy: 2.9 % / Rmerge(I) obs: 0.081 |
Reflection | *PLUS Num. measured all: 170722 / Rmerge(I) obs: 0.08 |
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Processing
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Refinement | Resolution: 2.25→8 Å /
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Refine analyze | Luzzati coordinate error obs: 0.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.25→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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