+Open data
-Basic information
Entry | Database: PDB / ID: 1gcj | ||||||
---|---|---|---|---|---|---|---|
Title | N-TERMINAL FRAGMENT OF IMPORTIN-BETA | ||||||
Components | IMPORTIN BETA | ||||||
Keywords | TRANSPORT PROTEIN / HEAT REPEAT MOTIF / NUCLEAR PORE-TARGETING COMPLEX COMPONENT / nuclear import factor | ||||||
Function / homology | Function and homology information Regulation of cholesterol biosynthesis by SREBP (SREBF) / Assembly of the ORC complex at the origin of replication / Apoptosis induced DNA fragmentation / Initiation of Nuclear Envelope (NE) Reformation / RNA import into nucleus / Interferon alpha/beta signaling / mitotic chromosome movement towards spindle pole / endoplasmic reticulum tubular network / establishment of mitotic spindle localization / astral microtubule organization ...Regulation of cholesterol biosynthesis by SREBP (SREBF) / Assembly of the ORC complex at the origin of replication / Apoptosis induced DNA fragmentation / Initiation of Nuclear Envelope (NE) Reformation / RNA import into nucleus / Interferon alpha/beta signaling / mitotic chromosome movement towards spindle pole / endoplasmic reticulum tubular network / establishment of mitotic spindle localization / astral microtubule organization / importin-alpha family protein binding / ribosomal protein import into nucleus / NLS-dependent protein nuclear import complex / nuclear import signal receptor activity / nuclear localization sequence binding / mitotic metaphase chromosome alignment / NLS-bearing protein import into nucleus / Maturation of hRSV A proteins / kinesin binding / mitotic spindle assembly / nuclear pore / Neutrophil degranulation / Hsp90 protein binding / small GTPase binding / cytoplasmic stress granule / protein import into nucleus / nuclear membrane / protein domain specific binding / protein-containing complex binding / protein-containing complex / nucleoplasm / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.6 Å | ||||||
Authors | Lee, S.J. / Imamoto, N. / Sakai, H. / Nakagawa, A. / Kose, S. / Koike, M. / Yamamoto, M. / Kumasaka, T. / Yoneda, Y. / Tsukihara, T. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2000 Title: The adoption of a twisted structure of importin-beta is essential for the protein-protein interaction required for nuclear transport. Authors: Lee, S.J. / Imamoto, N. / Sakai, H. / Nakagawa, A. / Kose, S. / Koike, M. / Yamamoto, M. / Kumasaka, T. / Yoneda, Y. / Tsukihara, T. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1gcj.cif.gz | 191.2 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1gcj.ent.gz | 154.4 KB | Display | PDB format |
PDBx/mmJSON format | 1gcj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1gcj_validation.pdf.gz | 380 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1gcj_full_validation.pdf.gz | 404.6 KB | Display | |
Data in XML | 1gcj_validation.xml.gz | 21 KB | Display | |
Data in CIF | 1gcj_validation.cif.gz | 32.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gc/1gcj ftp://data.pdbj.org/pub/pdb/validation_reports/gc/1gcj | HTTPS FTP |
-Related structure data
Related structure data | |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Details | The biological assembly is a monomer constructed from chain A or chain B. |
-Components
#1: Protein | Mass: 51878.734 Da / Num. of mol.: 2 / Fragment: N-TERMINAL DOMAIN (1-449 RESIDUES) Mutation: MET1MSE, MET146MSE,MET181MSE,MET219MSE,MET245MSE,MET252MSE,MET256MSE,MET268MSE,MET291MSE,MET353MSE,MET388MSE,MET410MSE,MET417MSE, Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Strain: C57BL6 / Tissue: THYMUS / Plasmid: PGEX-2T / Production host: Escherichia coli (E. coli) / References: UniProt: P70168 #2: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.63 Å3/Da / Density % sol: 53 % | ||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 5.5 Details: cacodylate,PEG4000,glycerol, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7 Details: drop consists of equal amounts of protein and reservoir solutions | ||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL45XU / Wavelength: 0.9793 |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Feb 25, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9793 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→57.33 Å / Num. obs: 33562 / % possible obs: 99.5 % / Observed criterion σ(I): -3 / Redundancy: 8.1 % / Rmerge(I) obs: 0.072 / Net I/σ(I): 11.1 |
Reflection shell | Resolution: 2.6→2.69 Å / Redundancy: 7.3 % / Rmerge(I) obs: 0.293 / % possible all: 99.9 |
Reflection | *PLUS Num. measured all: 271717 |
Reflection shell | *PLUS % possible obs: 99.9 % / Mean I/σ(I) obs: 4.6 |
-Processing
Software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MAD / Resolution: 2.6→39.18 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
| ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→39.18 Å
| ||||||||||||||||||||
Refine LS restraints |
|