+Open data
-Basic information
Entry | Database: PDB / ID: 2j3w | ||||||
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Title | The crystal structure of the bet3-trs31-sedlin complex. | ||||||
Components |
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Keywords | TRANSPORT / MULTISUBUNIT TETHERING FACTOR / TRAPP / PALMITATE / LIPOPROTEIN / ER-GOLGI TRANSPORT / ENDOPLASMIC RETICULUM / TRANSCRIPTION / GOLGI APPARATUS / VESICLE TRANSPORT | ||||||
Function / homology | Function and homology information COPII-mediated vesicle transport / vesicle coating / vesicle tethering / RAB GEFs exchange GTP for GDP on RABs / TRAPPI protein complex / COPII-mediated vesicle transport / TRAPPII protein complex / TRAPPIII protein complex / TRAPP complex / cis-Golgi network membrane ...COPII-mediated vesicle transport / vesicle coating / vesicle tethering / RAB GEFs exchange GTP for GDP on RABs / TRAPPI protein complex / COPII-mediated vesicle transport / TRAPPII protein complex / TRAPPIII protein complex / TRAPP complex / cis-Golgi network membrane / COPII vesicle coating / intra-Golgi vesicle-mediated transport / endoplasmic reticulum-Golgi intermediate compartment / endoplasmic reticulum to Golgi vesicle-mediated transport / transcription corepressor binding / Golgi membrane / positive regulation of gene expression / perinuclear region of cytoplasm / endoplasmic reticulum / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | MUS MUSCULUS (house mouse) BRACHYDANIO RERIO (zebrafish) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Kim, Y.-G. / Oh, B.-H. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 2006 Title: The Architecture of the Multisubunit Trapp I Complex Suggests a Model for Vesicle Tethering. Authors: Kim, Y.-G. / Raunser, S. / Munger, C. / Wagner, J. / Song, Y.-L. / Cygler, M. / Walz, T. / Oh, B.-H. / Sacher, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2j3w.cif.gz | 191 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2j3w.ent.gz | 158.9 KB | Display | PDB format |
PDBx/mmJSON format | 2j3w.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/j3/2j3w ftp://data.pdbj.org/pub/pdb/validation_reports/j3/2j3w | HTTPS FTP |
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-Related 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: 16705.027 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) MUS MUSCULUS (house mouse) / Plasmid: PPROEXHTA, PET15B, PET30A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q9CQP2 #2: Protein | Mass: 21059.367 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) BRACHYDANIO RERIO (zebrafish) / Plasmid: PPROEXHTA, PET15B, PET30A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q6DGL5 #3: Protein | Mass: 20452.227 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) MUS MUSCULUS (house mouse) / Plasmid: PPROEXHTA, PET15B, PET30A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O55013 #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 47 % |
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Crystal grow | pH: 8 Details: 20% (W/V) PEG3350, 0.2 M MGCL2, 2% (W/V) BENZAMIDINE AND 0.1 M TRIS HCL (PH 8.0) |
-Data collection
Diffraction | Mean temperature: 103 K |
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Diffraction source | Source: SYNCHROTRON / Site: PAL/PLS / Beamline: 4A / Wavelength: 1 |
Detector | Type: ADSC CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→30 Å / Num. obs: 57111 / % possible obs: 93 % / Observed criterion σ(I): 0 / Redundancy: 5.1 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 29 |
Reflection shell | Highest resolution: 2.1 Å / Mean I/σ(I) obs: 4.2 / % possible all: 73.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.1→30 Å / Data cutoff high absF: 10000 / Cross valid method: THROUGHOUT / σ(F): 1
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Solvent computation | Bsol: 39.3699 Å2 / ksol: 0.347067 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.1→30 Å
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Refine LS restraints |
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Xplor file |
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