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Open data
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Basic information
Entry | Database: PDB / ID: 1hjk | ||||||
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Title | ALKALINE PHOSPHATASE MUTANT H331Q | ||||||
![]() | ALKALINE PHOSPHATASE | ||||||
![]() | HYDROLASE / ALKALINE PHOSPHATASE / 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 | ![]() | ||||||
![]() | Murphy, J.E. / Stec, B. / Ma, L. / Kantrowitz, E.R. | ||||||
![]() | ![]() Title: Trapping and visualization of a covalent enzyme-phosphate intermediate. Authors: Murphy, J.E. / Stec, B. / Ma, L. / Kantrowitz, E.R. #1: ![]() Title: Mutations at Positions 153 and 328 in Escherichia Coli Alkaline Phosphatase Provide Insight Towards the Structure and Function of Mammalian and Yeast Alkaline Phosphatases Authors: Murphy, J.E. / Tibbitts, T.T. / Kantrowitz, E.R. #2: ![]() 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. #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 | ![]() | 179.3 KB | Display | ![]() |
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PDB format | ![]() | 149 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 400 KB | Display | ![]() |
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Full document | ![]() | 424.5 KB | Display | |
Data in XML | ![]() | 22.1 KB | Display | |
Data in CIF | ![]() | 36 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 on special symmetry positions |
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Noncrystallographic symmetry (NCS) | NCS domain:
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Components
#1: Protein | Mass: 47164.359 Da / Num. of mol.: 2 / Mutation: H331Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-ZN / #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: 3.35 Å3/Da / Density % sol: 63.27 % |
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Crystal grow | pH: 7.5 Details: 55% SATURATING (NH4)2SO4, 100 MM TRIS, 10 MM MGCL2, 10 MM ZNCL2, 2 MM NAH2PO4 AT PH 7.5 |
Crystal grow | *PLUS pH: 5.5 / Method: unknown |
Components of the solutions | *PLUS Conc.: 0.1 M / Common name: sodium acetate |
-Data collection
Diffraction | Mean temperature: 295 K |
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Diffraction source | Source: ![]() |
Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR / Date: Nov 1, 1995 |
Radiation | Monochromator: Y / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→80 Å / Num. obs: 51270 / % possible obs: 90 % / Observed criterion σ(I): 1 / Redundancy: 2.4 % / Rmerge(I) obs: 0.09 |
Reflection | *PLUS Num. measured all: 120731 / Rmerge(I) obs: 0.09 |
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Processing
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Refinement | Resolution: 2.3→8 Å / σ(F): 2
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Displacement parameters | Biso mean: 13.15 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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Refine LS restraints |
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Refine LS restraints NCS |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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