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- PDB-1inp: CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 1-PHOSPHATASE AT 2.3 ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1inp | ||||||
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Title | CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 1-PHOSPHATASE AT 2.3 ANGSTROMS RESOLUTION | ||||||
![]() | INOSITOL POLYPHOSPHATE 1-PHOSPHATASE | ||||||
![]() | HYDROLASE(PHOSPHORIC MONOESTER) | ||||||
Function / homology | ![]() inositol-1,3,4-trisphosphate 1-phosphatase activity / Synthesis of IP2, IP, and Ins in the cytosol / inositol-1,4-bisphosphate 1-phosphatase / inositol-1,4-bisphosphate 1-phosphatase activity / phosphatidylinositol phosphate biosynthetic process / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | York, J.D. / Ponder, J.W. / Chen, Z. / Mathews, F.S. / Majerus, P.W. | ||||||
![]() | ![]() Title: Crystal structure of inositol polyphosphate 1-phosphatase at 2.3-A resolution. Authors: York, J.D. / Ponder, J.W. / Chen, Z.W. / Mathews, F.S. / Majerus, P.W. #1: ![]() Title: Crystallization and Initial X-Ray Crystallographic Characterization of Recombinant Bovine Inositol Polyphosphate 1-Phosphatase Produced in Spodoptera Frugiperda Cells Authors: York, J.D. / Chen, Z. / Ponder, J.W. / Chauhan, A.K. / Mathews, F.S. / Majerus, P.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 | ![]() | 108 KB | Display | ![]() |
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PDB format | ![]() | 83.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 368.9 KB | Display | ![]() |
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Full document | ![]() | 390.6 KB | Display | |
Data in XML | ![]() | 11.6 KB | Display | |
Data in CIF | ![]() | 16.8 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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Atom site foot note | 1: CIS PROLINE - PRO 134 2: LEU 234 - PRO 235 OMEGA = 136.45 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
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Components
#1: Protein | Mass: 43976.934 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P21327, inositol-1,4-bisphosphate 1-phosphatase | ||||
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#2: Chemical | #3: Water | ChemComp-HOH / | Compound details | THE STRUCTURE OF 1-PTASE IS SIMILAR TO TWO OTHER MAGNESIUM DEPENDENT/LITHIUM SENSITIVE PHOSPHATASES: ...THE STRUCTURE OF 1-PTASE IS SIMILAR TO TWO OTHER MAGNESIUM DEPENDENT/LITHIUM SENSITIVE PHOSPHATAS | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.17 Å3/Da / Density % sol: 43.37 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / 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: 17652 / Observed criterion σ(I): 2 |
Reflection | *PLUS Highest resolution: 2.3 Å / % possible obs: 99.3 % / Num. measured all: 63687 / Rmerge F obs: 0.049 |
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Processing
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Refinement | Resolution: 2.3→8 Å / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.198 / Rfactor Rwork: 0.198 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 36.28 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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