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Yorodumi- PDB-2eqb: Crystal structure of the Rab GTPase Sec4p, the Sec2p GEF domain, ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2eqb | ||||||
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Title | Crystal structure of the Rab GTPase Sec4p, the Sec2p GEF domain, and phosphate complex | ||||||
Components |
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Keywords | ENDOCYTOSIS/EXOCYTOSIS / coiled coil / ENDOCYTOSIS-EXOCYTOSIS COMPLEX | ||||||
Function / homology | Function and homology information ascospore-type prospore assembly / Golgi to plasma membrane transport vesicle / Anchoring of the basal body to the plasma membrane / membrane addition at site of cytokinesis / RAB geranylgeranylation / RAB GEFs exchange GTP for GDP on RABs / cell tip / incipient cellular bud site / vesicle fusion / cellular bud tip ...ascospore-type prospore assembly / Golgi to plasma membrane transport vesicle / Anchoring of the basal body to the plasma membrane / membrane addition at site of cytokinesis / RAB geranylgeranylation / RAB GEFs exchange GTP for GDP on RABs / cell tip / incipient cellular bud site / vesicle fusion / cellular bud tip / Golgi to plasma membrane transport / vesicle docking involved in exocytosis / cellular bud neck / regulation of exocytosis / mating projection tip / phosphatidylinositol-4-phosphate binding / transport vesicle membrane / exocytosis / protein secretion / transport vesicle / Neutrophil degranulation / guanyl-nucleotide exchange factor activity / protein localization to plasma membrane / autophagy / protein transport / vesicle / mitochondrial outer membrane / endosome / GTPase activity / GTP binding / endoplasmic reticulum / mitochondrion / identical protein binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.7 Å | ||||||
Authors | Sato, Y. / Fukai, S. / Ishitani, R. / Nureki, O. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.Usa / Year: 2007 Title: Crystal structure of the Sec4p{middle dot}Sec2p complex in the nucleotide exchanging intermediate state Authors: Sato, Y. / Fukai, S. / Ishitani, R. / Nureki, O. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2eqb.cif.gz | 87.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2eqb.ent.gz | 67 KB | Display | PDB format |
PDBx/mmJSON format | 2eqb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eq/2eqb ftp://data.pdbj.org/pub/pdb/validation_reports/eq/2eqb | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 19447.211 Da / Num. of mol.: 1 / Fragment: residues 19-187 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Plasmid: pGEX-6P-1 / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta (DE3) / References: UniProt: P07560 | ||||
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#2: Protein | Mass: 11391.563 Da / Num. of mol.: 2 / Fragment: GEF domain, residues 51-142 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Plasmid: pGEX-6P-1 / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta (DE3) / References: UniProt: P17065 #3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 5 Å3/Da / Density % sol: 75.2 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.2 Details: 150mM Dipotassium hydrogenphosphate, 17% PEG 3350, 150mM dimethyl(2-hydroxyethyl)ammonium propane sulfonate, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation |
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Radiation wavelength |
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Reflection | Resolution: 2.7→50 Å / Num. all: 23619 / Num. obs: 23619 / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Biso Wilson estimate: 27.6 Å2 / Net I/σ(I): 12.7 | ||||||||||||||||||
Reflection shell | Resolution: 2.7→2.75 Å / Mean I/σ(I) obs: 2.07 / Rsym value: 0.288 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.7→48.08 Å / Rfactor Rfree error: 0.009 / Data cutoff high absF: 3233822.84 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 40.4236 Å2 / ksol: 0.307169 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 77.7 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.7→48.08 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.7→2.87 Å / Rfactor Rfree error: 0.032 / Total num. of bins used: 6
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Xplor file |
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