+Open data
-Basic information
Entry | Database: PDB / ID: 1byu | ||||||
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Title | CANINE GDP-RAN | ||||||
Components | PROTEIN (GTP-BINDING PROTEIN RAN) | ||||||
Keywords | TRANSPORT PROTEIN / GTPASE / NUCLEAR TRANSPORT | ||||||
Function / homology | Function and homology information RISC complex binding / pre-miRNA binding / pre-miRNA export from nucleus / nuclear export signal receptor activity / snRNA import into nucleus / RISC complex / GTP metabolic process / mitotic sister chromatid segregation / ribosomal subunit export from nucleus / protein export from nucleus ...RISC complex binding / pre-miRNA binding / pre-miRNA export from nucleus / nuclear export signal receptor activity / snRNA import into nucleus / RISC complex / GTP metabolic process / mitotic sister chromatid segregation / ribosomal subunit export from nucleus / protein export from nucleus / positive regulation of protein export from nucleus / protein import into nucleus / melanosome / nuclear envelope / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / cell division / GTPase activity / GTP binding / magnesium ion binding / protein-containing complex / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Canis lupus familiaris (dog) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.15 Å | ||||||
Authors | Stewart, M. / Kent, H.M. / Mccoy, A.J. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1998 Title: The structure of the Q69L mutant of GDP-Ran shows a major conformational change in the switch II loop that accounts for its failure to bind nuclear transport factor 2 (NTF2). Authors: Stewart, M. / Kent, H.M. / McCoy, A.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1byu.cif.gz | 100.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1byu.ent.gz | 77.1 KB | Display | PDB format |
PDBx/mmJSON format | 1byu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1byu_validation.pdf.gz | 512.4 KB | Display | wwPDB validaton report |
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Full document | 1byu_full_validation.pdf.gz | 518 KB | Display | |
Data in XML | 1byu_validation.xml.gz | 10.4 KB | Display | |
Data in CIF | 1byu_validation.cif.gz | 16.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/by/1byu ftp://data.pdbj.org/pub/pdb/validation_reports/by/1byu | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.18639, -0.0947, 0.9779), Vector: |
-Components
#1: Protein | Mass: 24482.143 Da / Num. of mol.: 2 / Fragment: ALL Source method: isolated from a genetically manipulated source Source: (gene. exp.) Canis lupus familiaris (dog) / Species: Canis lupus / Strain: BL21(DE3) / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P62825 #2: Chemical | #3: Chemical | #4: 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: 2.25 Å3/Da / Density % sol: 32 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.2 / Details: SEE PUBLICATION, pH 7.2 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / pH: 8 / Method: vapor diffusion | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ELETTRA / Beamline: 5.2R / Wavelength: 1.0378 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jan 29, 1998 / Details: MIRRORS |
Radiation | Monochromator: CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0378 Å / Relative weight: 1 |
Reflection | Resolution: 2.15→21.3 Å / Num. obs: 22596 / % possible obs: 94.7 % / Redundancy: 2 % / Rmerge(I) obs: 0.03 / Net I/σ(I): 20.9 |
Reflection shell | Resolution: 2.15→2.27 Å / Redundancy: 2 % / Rmerge(I) obs: 0.097 / Mean I/σ(I) obs: 7.6 / % possible all: 92.2 |
Reflection | *PLUS Num. measured all: 45779 |
Reflection shell | *PLUS % possible obs: 92.2 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: SCHEFFZEK ET AL Resolution: 2.15→6 Å / σ(F): 0 / ESU R: 0.3 / ESU R Free: 0.23
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Displacement parameters | Biso mean: 32.95 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.15→6 Å
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Refine LS restraints |
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