+Open data
-Basic information
Entry | Database: PDB / ID: 2d4c | ||||||
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Title | Crystal structure of the endophilin BAR domain mutant | ||||||
Components | SH3-containing GRB2-like protein 2 | ||||||
Keywords | TRANSFERASE / BAR domain | ||||||
Function / homology | Function and homology information negative regulation of blood-brain barrier permeability / synaptic vesicle uncoating / dendrite extension / Retrograde neurotrophin signalling / Lysosome Vesicle Biogenesis / Golgi Associated Vesicle Biogenesis / Recycling pathway of L1 / cellular response to brain-derived neurotrophic factor stimulus / MHC class II antigen presentation / InlB-mediated entry of Listeria monocytogenes into host cell ...negative regulation of blood-brain barrier permeability / synaptic vesicle uncoating / dendrite extension / Retrograde neurotrophin signalling / Lysosome Vesicle Biogenesis / Golgi Associated Vesicle Biogenesis / Recycling pathway of L1 / cellular response to brain-derived neurotrophic factor stimulus / MHC class II antigen presentation / InlB-mediated entry of Listeria monocytogenes into host cell / negative regulation of protein phosphorylation / central nervous system development / cell projection / EGFR downregulation / clathrin-coated endocytic vesicle membrane / Negative regulation of MET activity / neuron projection development / Cargo recognition for clathrin-mediated endocytosis / presynapse / Clathrin-mediated endocytosis / early endosome / Golgi membrane / negative regulation of gene expression / lipid binding / glutamatergic synapse / perinuclear region of cytoplasm / signal transduction / identical protein binding / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Masuda, M. / Takeda, S. | ||||||
Citation | Journal: Embo J. / Year: 2006 Title: Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms Authors: Masuda, M. / Takeda, S. / Sone, M. / Ohki, T. / Mori, H. / Kamioka, Y. / Mochizuki, N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2d4c.cif.gz | 190.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2d4c.ent.gz | 152.7 KB | Display | PDB format |
PDBx/mmJSON format | 2d4c.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/d4/2d4c ftp://data.pdbj.org/pub/pdb/validation_reports/d4/2d4c | HTTPS FTP |
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-Related structure data
Related structure data | 1x03SC 1x04C S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-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: 29056.242 Da / Num. of mol.: 4 / Fragment: endophilin A1 BAR domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pGEX6p3 / Production host: Escherichia coli (E. coli) / Strain (production host): XL10-Gold References: UniProt: Q99962, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups #2: Chemical | ChemComp-CA / | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.18 Å3/Da / Density % sol: 43.55 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.2 Details: 100mM HEPES, 200mM calcium acetate, 10mM DTT, 20% PEG3350, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 90 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL38B1 / Wavelength: 1 Å |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Jun 6, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→50 Å / Num. obs: 38763 / % possible obs: 99.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.8 % / Rmerge(I) obs: 0.098 / Net I/σ(I): 11 |
Reflection shell | Resolution: 2.4→2.49 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.323 / Num. unique all: 3673 / % possible all: 93.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 1X03 Resolution: 2.4→50 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.4→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.4→2.49 Å
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