+
Open data
-
Basic information
Entry | Database: PDB / ID: 9f5f | ||||||
---|---|---|---|---|---|---|---|
Title | UP1 in complex with Z992569480 | ||||||
![]() | Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed | ||||||
![]() | RNA BINDING PROTEIN / fragment screening / hnRNP A1 / UP1 / RNA/DNA BINDING PROTEIN / UP1-fragment complex | ||||||
Function / homology | ![]() cellular response to sodium arsenite / SARS-CoV-1-host interactions / import into nucleus / telomeric repeat-containing RNA binding / pre-mRNA binding / G-rich strand telomeric DNA binding / nuclear export / RNA export from nucleus / miRNA binding / FGFR2 alternative splicing ...cellular response to sodium arsenite / SARS-CoV-1-host interactions / import into nucleus / telomeric repeat-containing RNA binding / pre-mRNA binding / G-rich strand telomeric DNA binding / nuclear export / RNA export from nucleus / miRNA binding / FGFR2 alternative splicing / regulation of alternative mRNA splicing, via spliceosome / SARS-CoV-1 modulates host translation machinery / regulation of RNA splicing / Processing of Capped Intron-Containing Pre-mRNA / negative regulation of telomere maintenance via telomerase / mRNA transport / cellular response to glucose starvation / positive regulation of telomere maintenance via telomerase / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / mRNA 3'-UTR binding / spliceosomal complex / mRNA splicing, via spliceosome / single-stranded DNA binding / single-stranded RNA binding / ribonucleoprotein complex / protein domain specific binding / DNA binding / RNA binding / extracellular exosome / nucleoplasm / identical protein binding / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Dunnett, L. / Prischi, F. | ||||||
Funding support | 1items
| ||||||
![]() | ![]() Title: Enhanced identification of small molecules binding to hnRNP A1 via in silico hotspot and cryptic pockets mapping coupled with X-Ray fragment screening Authors: Dunnett, L. / Prischi, F. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 59.5 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 37.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 649.6 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 650.2 KB | Display | |
Data in XML | ![]() | 10.9 KB | Display | |
Data in CIF | ![]() | 16.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9f4dC ![]() 9f4eC ![]() 9f4fC ![]() 9f4gC ![]() 9f4hC ![]() 9f4jC ![]() 9f4kC ![]() 9f4lC ![]() 9f4mC ![]() 9f4nC ![]() 9f4oC ![]() 9f4pC ![]() 9f4qC ![]() 9f4rC ![]() 9f4sC ![]() 9f4tC ![]() 9f4uC ![]() 9f4vC ![]() 9f4wC ![]() 9f4xC ![]() 9f4yC ![]() 9f4zC ![]() 9f50C ![]() 9f51C ![]() 9f52C ![]() 9f53C ![]() 9f54C ![]() 9f55C ![]() 9f5cC ![]() 9f5dC ![]() 9f5eC ![]() 9f5gC ![]() 9f5kC ![]() 9f7fC ![]() 9f7hC C: citing same article ( |
---|---|
Similar structure data | Similarity search - Function & homology ![]() |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 22357.109 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|---|
#2: Chemical | ChemComp-W0J / ( |
#3: Water | ChemComp-HOH / |
Has ligand of interest | Y |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.07 Å3/Da / Density % sol: 40.64 % |
---|---|
Crystal grow | Temperature: 289 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: 0.1 M Tris-HCl, pH 8.50, 25% PEG-4000, 8% 2-Methyl-2,4-pentanediol |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Jun 29, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91587 Å / Relative weight: 1 |
Reflection | Resolution: 1.4→32.46 Å / Num. obs: 35726 / % possible obs: 98.4 % / Redundancy: 1.7 % / Biso Wilson estimate: 11.98 Å2 / CC1/2: 0.986 / Rmerge(I) obs: 0.058 / Rpim(I) all: 0.058 / Rrim(I) all: 0.082 / Χ2: 0.73 / Net I/σ(I): 7.8 / Num. measured all: 62386 |
Reflection shell | Resolution: 1.4→1.42 Å / Redundancy: 1.3 % / Mean I/σ(I) obs: 4 / Num. unique obs: 1525 / CC1/2: 0.913 / % possible all: 85.4 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 16.42 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.4→32.46 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell |
|