+Open data
-Basic information
Entry | Database: PDB / ID: 4v0m | ||||||
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Title | Crystal structure of BBS1N in complex with ARL6DN | ||||||
Components |
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Keywords | HYDROLASE/STRUCTURAL PROTEIN / HYDROLASE-STRUCTURAL PROTEIN COMPLEX / BBSOME / GTP / COAT COMPLEX | ||||||
Function / homology | Function and homology information BBSome / protein localization to cilium / non-motile cilium assembly / axoneme / cilium assembly / vesicle-mediated transport / intracellular protein transport / GTPase activity / GTP binding Similarity search - Function | ||||||
Biological species | CHLAMYDOMONAS REINHARDTII (plant) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / OTHER / Resolution: 3.45 Å | ||||||
Authors | Mourao, A. / Lorentzen, E. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2014 Title: Structural Basis for Membrane Targeting of the Bbsome by Arl6 Authors: Mourao, A. / Nager, A.R. / Nachury, M.V. / Lorentzen, E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4v0m.cif.gz | 371 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4v0m.ent.gz | 306.2 KB | Display | PDB format |
PDBx/mmJSON format | 4v0m.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v0/4v0m ftp://data.pdbj.org/pub/pdb/validation_reports/v0/4v0m | 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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3 |
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4 |
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Unit cell |
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-Components
#1: Protein | Mass: 18806.646 Da / Num. of mol.: 3 / Fragment: GTPASE, RESIDUES 16-180 Source method: isolated from a genetically manipulated source Source: (gene. exp.) CHLAMYDOMONAS REINHARDTII (plant) / Cell line (production host): High Five / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: A8JF99 #2: Protein | Mass: 46368.062 Da / Num. of mol.: 4 / Fragment: WD40, RESIDUES 1-425 Source method: isolated from a genetically manipulated source Source: (gene. exp.) CHLAMYDOMONAS REINHARDTII (plant) / Cell line (production host): High Five / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: A8JEA1 #3: Protein | | Mass: 18806.646 Da / Num. of mol.: 1 / Fragment: GTPASE, RESIDUES 16-180 Source method: isolated from a genetically manipulated source Source: (gene. exp.) CHLAMYDOMONAS REINHARDTII (plant) / Cell line (production host): High Five / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: A8JF99 #4: Chemical | ChemComp-GTP / #5: Chemical | ChemComp-MG / |
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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: 3.89 Å3/Da / Density % sol: 68.39 % / Description: NONE |
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Crystal grow | Details: 29% PEG400, 0.1M TRIS PH 8 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 |
Detector | Type: DECTRIS PILATUS 2MF / Detector: PIXEL |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.45→50 Å / Num. obs: 51878 / % possible obs: 99.1 % / Observed criterion σ(I): 1 / Redundancy: 6.5 % / Biso Wilson estimate: 129.02 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 9.1 |
Reflection shell | Resolution: 3.45→3.55 Å / Redundancy: 6 % / Rmerge(I) obs: 0.82 / Mean I/σ(I) obs: 1 / % possible all: 97.6 |
-Processing
Software |
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Refinement | Method to determine structure: OTHER Starting model: NONE Resolution: 3.45→87.128 Å / SU ML: 0.66 / σ(F): 1.87 / Phase error: 32.44 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.45→87.128 Å
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Refine LS restraints |
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LS refinement shell |
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