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Open data
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Basic information
Entry | Database: PDB / ID: 3ran | ||||||
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Title | CANINE GDP-RAN Q69L MUTANT | ||||||
![]() | PROTEIN (GTP-BINDING NUCLEAR PROTEIN RAN) | ||||||
![]() | TRANSPORT PROTEIN / GTPASE / NUCLEAR TRANSPORT | ||||||
Function / homology | ![]() RISC complex binding / pre-miRNA binding / pre-miRNA export from nucleus / nuclear export signal receptor activity / snRNA import into nucleus / GTP metabolic process / RISC complex / 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 / GTP metabolic process / RISC complex / mitotic sister chromatid segregation / ribosomal subunit export from nucleus / protein export from nucleus / positive regulation of protein export from nucleus / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein import into nucleus / melanosome / nuclear envelope / cell division / GTPase activity / GTP binding / magnesium ion binding / protein-containing complex / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Stewart, M. / Kent, H.M. / Mccoy, A.J. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 181.4 KB | Display | ![]() |
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PDB format | ![]() | 144.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 630.1 KB | Display | ![]() |
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Full document | ![]() | 646.7 KB | Display | |
Data in XML | ![]() | 19.7 KB | Display | |
Data in CIF | ![]() | 29.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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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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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 24441.135 Da / Num. of mol.: 4 / Mutation: Q69L Source method: isolated from a genetically manipulated source Details: Q69L MUTANT CONSTRUCTED BY PROTEIN ENGINEERING / Source: (gene. exp.) ![]() ![]() Description: CDNA OBTAINED BY SITE-SPECIFIC MUTAGENESIS OF WILD-TYPE CANINE RAN CDNA AS DESCRIBED IN PUBLICATION Species (production host): Escherichia coli / Production host: ![]() ![]() #2: Chemical | ChemComp-MG / #3: Chemical | ChemComp-GDP / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.18 Å3/Da / Density % sol: 43.63 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.2 / Details: SEE PUBLICATION, pH 7.2 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / pH: 7.4 / 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: ![]() ![]() ![]() |
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: 2.3→32.3 Å / Num. obs: 35632 / % possible obs: 94.7 % / Redundancy: 2.1 % / Rmerge(I) obs: 0.035 / Net I/σ(I): 14.8 |
Reflection shell | Resolution: 2.3→2.42 Å / Redundancy: 2.1 % / Rmerge(I) obs: 0.155 / Mean I/σ(I) obs: 4.9 / % possible all: 94.9 |
Reflection | *PLUS Num. measured all: 76123 |
Reflection shell | *PLUS % possible obs: 94.9 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: EBI-1279 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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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.3 Å / Rfactor Rfree: 0.271 / Rfactor Rwork: 0.201 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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