+Open data
-Basic information
Entry | Database: PDB / ID: 5hb5 | ||||||||||||||||||||||||||||||
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Title | Crystal structure of Chaetomium thermophilum Nup145N APD | ||||||||||||||||||||||||||||||
Components | Nucleoporin NUP145 | ||||||||||||||||||||||||||||||
Keywords | TRANSPORT PROTEIN / Nucleocytoplasmic transport / Protein transport | ||||||||||||||||||||||||||||||
Function / homology | Function and homology information structural constituent of nuclear pore / Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / mRNA transport / nuclear pore / protein transport / nuclear membrane / hydrolase activity / RNA binding Similarity search - Function | ||||||||||||||||||||||||||||||
Biological species | Chaetomium thermophilum (fungus) | ||||||||||||||||||||||||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.5 Å | ||||||||||||||||||||||||||||||
Authors | Lin, D.H. / Stuwe, T. / Hoelz, A. | ||||||||||||||||||||||||||||||
Funding support | United States, Germany, China, 9items
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Citation | Journal: Science / Year: 2016 Title: Architecture of the symmetric core of the nuclear pore. Authors: Lin, D.H. / Stuwe, T. / Schilbach, S. / Rundlet, E.J. / Perriches, T. / Mobbs, G. / Fan, Y. / Thierbach, K. / Huber, F.M. / Collins, L.N. / Davenport, A.M. / Jeon, Y.E. / Hoelz, A. | ||||||||||||||||||||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5hb5.cif.gz | 185.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5hb5.ent.gz | 153.1 KB | Display | PDB format |
PDBx/mmJSON format | 5hb5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hb/5hb5 ftp://data.pdbj.org/pub/pdb/validation_reports/hb/5hb5 | HTTPS FTP |
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-Related structure data
Related structure data | 5haxC 5hayC 5hazC 5hb0C 5hb1C 5hb2C 5hb3C 5hb4C 5hb6C 5hb7C 5hb8C C: citing same article (ref.) |
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Similar 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: 15693.921 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (fungus) Strain: DSM 1495 / CBS 144.50 / IMI 039719 / Gene: NUP145, CTHT_0042590 / Production host: Escherichia coli (E. coli) References: UniProt: G0SAK3, Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases #2: Chemical | ChemComp-FLC / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 1.97 Å3/Da / Density % sol: 37.68 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, hanging drop / Details: 0.1 M citric acid (pH 3.0), 25 % (w/v) PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL12-2 / Wavelength: 0.9795 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Apr 20, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→30 Å / Num. obs: 38743 / % possible obs: 97.2 % / Redundancy: 6.6 % / Net I/σ(I): 12.4 |
-Processing
Software |
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Refinement | Resolution: 1.5→27.663 Å / SU ML: 0.15 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 24.15 / 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: 1.5→27.663 Å
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Refine LS restraints |
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LS refinement shell |
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