+Open data
-Basic information
Entry | Database: PDB / ID: 1xti | ||||||
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Title | Structure of Wildtype human UAP56 | ||||||
Components | Probable ATP-dependent RNA helicase p47 | ||||||
Keywords | GENE REGULATION / alpha-beta fold | ||||||
Function / homology | Function and homology information transcription export complex / U6 snRNP / RNA secondary structure unwinding / mRNA 3'-end processing / ATP-dependent activity, acting on RNA / ATP-dependent protein binding / U4 snRNA binding / Transport of Mature mRNA derived from an Intron-Containing Transcript / RNA export from nucleus / U4 snRNP ...transcription export complex / U6 snRNP / RNA secondary structure unwinding / mRNA 3'-end processing / ATP-dependent activity, acting on RNA / ATP-dependent protein binding / U4 snRNA binding / Transport of Mature mRNA derived from an Intron-Containing Transcript / RNA export from nucleus / U4 snRNP / RNA Polymerase II Transcription Termination / spliceosomal complex assembly / RHOBTB2 GTPase cycle / U6 snRNA binding / mRNA export from nucleus / mRNA Splicing - Major Pathway / RNA splicing / spliceosomal complex / mRNA splicing, via spliceosome / RNA helicase activity / RNA helicase / nuclear speck / ATP hydrolysis activity / RNA binding / nucleoplasm / ATP binding / identical protein binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.95 Å | ||||||
Authors | Shi, H. / Cordin, O. / Minder, C.M. / Linder, P. / Xu, R.M. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.Usa / Year: 2004 Title: Crystal structure of the human ATP-dependent splicing and export factor UAP56 Authors: Shi, H. / Cordin, O. / Minder, C.M. / Linder, P. / Xu, R.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1xti.cif.gz | 96 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1xti.ent.gz | 71.2 KB | Display | PDB format |
PDBx/mmJSON format | 1xti.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xt/1xti ftp://data.pdbj.org/pub/pdb/validation_reports/xt/1xti | HTTPS FTP |
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-Related structure data
Related structure data | 1xtjC 1xtkC 1fukS 1qdeS S: Starting model for refinement 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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Unit cell |
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-Components
#1: Protein | Mass: 45069.141 Da / Num. of mol.: 1 / Fragment: sequence database residues 46-428 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: BAT1 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q13838 | ||
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#2: Chemical | ChemComp-IPA / #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50.2 % |
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 5% iso-propanol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X26C / Wavelength: 1.1 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Apr 6, 2002 |
Radiation | Monochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 1.95→50 Å / Num. obs: 28304 / % possible obs: 99 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 1.95→2.02 Å / % possible all: 96.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRIES 1FUK, 1QDE Resolution: 1.95→33.1 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.95→33.1 Å
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Refine LS restraints |
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Xplor file |
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