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Open data
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Basic information
Entry | Database: PDB / ID: 1ura | ||||||
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Title | ALKALINE PHOSPHATASE (D51ZN) | ||||||
![]() | ALKALINE PHOSPHATASE | ||||||
![]() | ALKALINE PHOSPHATASE / HYDROLASE / PHOSPHORIC MONOESTER / PHOSPHO TRANSFERASE / 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 | ![]() | ||||||
![]() | Tibbitts, T.T. / Murphy, J.E. / Kantrowitz, E.R. | ||||||
![]() | ![]() Title: Kinetic and structural consequences of replacing the aspartate bridge by asparagine in the catalytic metal triad of Escherichia coli alkaline phosphatase. Authors: Tibbitts, T.T. / Murphy, J.E. / 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 E. 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 | ![]() | 177.4 KB | Display | ![]() |
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PDB format | ![]() | 146.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 387.5 KB | Display | ![]() |
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Full document | ![]() | 401.9 KB | Display | |
Data in XML | ![]() | 20.1 KB | Display | |
Data in CIF | ![]() | 31.4 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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1 |
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Unit cell |
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Components on special symmetry positions |
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Details | THERE IS A DIMER (IDENTICAL CHAINS OF 449 RESIDUES) PER ASYMMETRIC UNIT. THESE SUBUNITS ARE DESIGNATED "A" AND "B". |
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Components
#1: Protein | Mass: 46766.074 Da / Num. of mol.: 2 / Mutation: D51N Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-ZN / #3: Chemical | ChemComp-PO4 / #4: Water | ChemComp-HOH / | Compound details | THE STRUCTURE IS OF A MUTANT ALKALINE PHOSPHATE (D51N) IN WHICH ASP-51 IS REPLACED BY ASN. THERE ...THE STRUCTURE IS OF A MUTANT ALKALINE PHOSPHATE (D51N) IN WHICH ASP-51 IS REPLACED BY ASN. THERE ARE TWO ZINCS COMPLEXED WITH AN INORGANIC PHOSPHATE BOUND IN EACH OF THE TWO ACTIVE SITES. THE THIRD METAL BIN SITE IS UNOCCUPIED | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.32 Å3/Da / Density % sol: 62.92 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 Details: 65% SATURATING (NH4)2SO4, 100 MM TRIS, 10 MM MGCL2, 10 MM ZNCL2, 2 MM NAH2PO4 AT PH 7.5. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 9.5 / Method: vapor diffusion, hanging drop / Details: Chen, L. C., (1992) Protein Eng., 5, 605. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Detector | Date: Jun 29, 1994 |
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Radiation | Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 73906 / % possible obs: 93.3 % / Observed criterion σ(I): 3 |
Reflection | *PLUS Highest resolution: 2.04 Å / Redundancy: 4.6 % / Num. measured all: 367482 / Rmerge(I) obs: 0.097 |
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Processing
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Refinement | Resolution: 2.04→8 Å / σ(F): 2
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Refine analyze | Luzzati coordinate error obs: 0.25 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.04→8 Å
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Refine LS restraints |
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Refine LS restraints | *PLUS
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