+Open data
-Basic information
Entry | Database: PDB / ID: 4c0p | ||||||
---|---|---|---|---|---|---|---|
Title | Unliganded Transportin 3 | ||||||
Components | TRANSPORTIN-3 | ||||||
Keywords | TRANSPORT PROTEIN / NUCLEAR IMPORT / HEAT REPEAT / TNPO3 | ||||||
Function / homology | Function and homology information annulate lamellae / nuclear import signal receptor activity / small GTPase binding / protein import into nucleus / nuclear envelope / intracellular membrane-bounded organelle / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.95 Å | ||||||
Authors | Maertens, G.N. / Cook, N.J. / Hare, S. / Cherepanov, P. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2014 Title: Structural Basis for Nuclear Import of Splicing Factors by Human Transportin 3. Authors: Maertens, G.N. / Cook, N.J. / Wang, W. / Hare, S. / Gupta, S.S. / Oztop, I. / Lee, K. / Pye, V.E. / Cosnefroy, O. / Snijders, A.P. / Kewalramani, V.N. / Fassati, A. / Engelman, A. / Cherepanov, P. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 4c0p.cif.gz | 689.4 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb4c0p.ent.gz | 567.6 KB | Display | PDB format |
PDBx/mmJSON format | 4c0p.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c0/4c0p ftp://data.pdbj.org/pub/pdb/validation_reports/c0/4c0p | HTTPS FTP |
---|
-Related structure data
Related structure data | 4c0oC 4c0qC 2x19S 2xwuS C: citing same article (ref.) S: Starting model for refinement |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||||||||
2 |
| ||||||||||||||||
3 |
| ||||||||||||||||
4 |
| ||||||||||||||||
Unit cell |
| ||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
|
-Components
#1: Protein | Mass: 104281.148 Da / Num. of mol.: 4 / Mutation: YES Source method: isolated from a genetically manipulated source Details: C511A MUTATION ENGINEERED TO IMPROVE CRYSTAL PACKING Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PETSUMO-TNPO3(C511A) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA2 LAC I / References: UniProt: Q9Y5L0 #2: Chemical | ChemComp-DTT / Sequence details | C511A MUTATION ENGINEERED | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.88 Å3/Da / Density % sol: 57.3 % / Description: NONE |
---|---|
Crystal grow | pH: 8.2 Details: 20% (W/V) PEG3350, 0.2 M NABR, 10 MM DTT, 2 MM EDTA, 0.1 M BIS-TRIS PROPANE, PH8.2 |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.9394 |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 15, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9394 Å / Relative weight: 1 |
Reflection | Resolution: 2.95→40 Å / Num. obs: 96311 / % possible obs: 98.6 % / Redundancy: 3.7 % / Biso Wilson estimate: 78.3 Å2 / Rmerge(I) obs: 0.14 / Net I/σ(I): 8.1 |
Reflection shell | Resolution: 2.95→3.11 Å / Redundancy: 3.9 % / Rmerge(I) obs: 1.13 / Mean I/σ(I) obs: 1.4 / % possible all: 98.7 |
-Processing
Software |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRIES 2X19, 2XWU Resolution: 2.95→38.17 Å / SU ML: 0.44 / σ(F): 1.96 / Phase error: 30.95 / Stereochemistry target values: ML
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 90.8 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.95→38.17 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell |
|