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- PDB-1djz: PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEX... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1djz | ||||||
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Title | PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEXED WITH INOSITOL-4,5-BISPHOSPHATE | ||||||
![]() | PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1 | ||||||
![]() | LIPID DEGRADATION / PHOSPHORIC DIESTER HYDROLASE / HYDROLASE / TRANSDUCER / CALCIUM-BINDING / PHOSPHOLIPASE C / PHOSPHOINOSITIDE-SPECIFIC | ||||||
Function / homology | ![]() Synthesis of IP3 and IP4 in the cytosol / response to prostaglandin F / positive regulation of inositol trisphosphate biosynthetic process / phosphoinositide phospholipase C / positive regulation of norepinephrine secretion / phosphatidylinositol phosphate binding / response to aluminum ion / phosphatidylinositol metabolic process / phosphatidylinositol phospholipase C activity / phosphatidic acid binding ...Synthesis of IP3 and IP4 in the cytosol / response to prostaglandin F / positive regulation of inositol trisphosphate biosynthetic process / phosphoinositide phospholipase C / positive regulation of norepinephrine secretion / phosphatidylinositol phosphate binding / response to aluminum ion / phosphatidylinositol metabolic process / phosphatidylinositol phospholipase C activity / phosphatidic acid binding / phospholipase C activity / inositol 1,4,5 trisphosphate binding / calcium-dependent phospholipid binding / GTPase activating protein binding / labyrinthine layer blood vessel development / phosphatidylinositol-mediated signaling / response to hyperoxia / lipid catabolic process / release of sequestered calcium ion into cytosol / : / regulation of cytosolic calcium ion concentration / phosphatidylinositol-4,5-bisphosphate binding / mitochondrial membrane / phospholipid binding / response to peptide hormone / response to calcium ion / phospholipase C-activating G protein-coupled receptor signaling pathway / regulation of cell population proliferation / angiogenesis / G protein-coupled receptor signaling pathway / calcium ion binding / enzyme binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Essen, L.-O. / Perisic, O. / Williams, R.L. | ||||||
![]() | ![]() Title: Structural mapping of the catalytic mechanism for a mammalian phosphoinositide-specific phospholipase C. Authors: Essen, L.O. / Perisic, O. / Katan, M. / Wu, Y. / Roberts, M.F. / Williams, R.L. #1: ![]() Title: Crystal Structure of a Mammalian Phosphoinositide-Specific Phospholipase C Delta Authors: Essen, L.O. / Perisic, O. / Cheung, R. / Katan, M. / Williams, R.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 232.7 KB | Display | ![]() |
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PDB format | ![]() | 185.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.3 MB | Display | |
Data in XML | ![]() | 50.2 KB | Display | |
Data in CIF | ![]() | 69.3 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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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 70574.516 Da / Num. of mol.: 2 / Mutation: DELTA(1-132) DELETION VARIANT Source method: isolated from a genetically manipulated source Details: CATALYTICALLY-ACTIVE DELETION VARIANT THAT LACKS AN N-TERMINAL PH DOMAIN, COMPLEXED WITH INOSITOL-4,5-BISPHOSPHATE Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P10688, phosphoinositide phospholipase C #2: Chemical | ChemComp-CA / #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: 4.6 Å3/Da / Density % sol: 70 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 12 ℃ / Method: vapor diffusion, hanging drop / Details: used to seeding | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 30, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.988 Å / Relative weight: 1 |
Reflection | Num. obs: 55796 / % possible obs: 94.8 % / Observed criterion σ(I): -3 / Redundancy: 5.9 % / Rmerge(I) obs: 0.091 |
Reflection | *PLUS Highest resolution: 2.95 Å / Lowest resolution: 37 Å / Num. measured all: 326969 |
Reflection shell | *PLUS % possible obs: 92.8 % / Redundancy: 4.6 % / Rmerge(I) obs: 0.326 |
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Processing
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Refinement | Resolution: 2.95→10 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 2.95→10 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Version: 5E / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.212 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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