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Open data
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Basic information
Entry | Database: PDB / ID: 1nmu | |||||||||
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Title | MBP-L30 | |||||||||
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![]() | SUGAR BINDING PROTEIN/RIBOSOME / structural flexibility / ribosomal protein L30 / MBP-L30 fusion protein / SUGAR BINDING PROTEIN-RIBOSOME COMPLEX | |||||||||
Function / homology | ![]() pre-mRNA 5'-splice site binding / detection of maltose stimulus / maltose transport complex / SRP-dependent cotranslational protein targeting to membrane / GTP hydrolysis and joining of the 60S ribosomal subunit / carbohydrate transport / Formation of a pool of free 40S subunits / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / negative regulation of mRNA splicing, via spliceosome ...pre-mRNA 5'-splice site binding / detection of maltose stimulus / maltose transport complex / SRP-dependent cotranslational protein targeting to membrane / GTP hydrolysis and joining of the 60S ribosomal subunit / carbohydrate transport / Formation of a pool of free 40S subunits / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / negative regulation of mRNA splicing, via spliceosome / L13a-mediated translational silencing of Ceruloplasmin expression / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / ATP-binding cassette (ABC) transporter complex / cell chemotaxis / rRNA processing / outer membrane-bounded periplasmic space / cytosolic large ribosomal subunit / periplasmic space / cytoplasmic translation / structural constituent of ribosome / DNA damage response / RNA binding / membrane / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Chao, J.A. / Prasad, G.S. / White, S.A. / Stout, C.D. / Williamson, J.R. | |||||||||
![]() | ![]() Title: Inherent Protein Structural Flexibility at the RNA-binding Interface of L30e Authors: Chao, J.A. / Prasad, G.S. / White, S.A. / Stout, C.D. / Williamson, J.R. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 194.2 KB | Display | ![]() |
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PDB format | ![]() | 155.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 519.2 KB | Display | ![]() |
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Full document | ![]() | 552.9 KB | Display | |
Data in XML | ![]() | 23.6 KB | Display | |
Data in CIF | ![]() | 36 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 41841.266 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein | Mass: 11299.168 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() #3: Polysaccharide | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.41 Å3/Da / Density % sol: 63.92 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7 Details: Sodium Citrate, Tris, Sodium Chloride, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 295K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 22 ℃ / pH: 6.2 | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Nov 16, 2000 / Details: double crystal monochromater |
Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 2.31→18 Å / Num. all: 65857 / Num. obs: 65330 / % possible obs: 99.2 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 |
Reflection shell | Resolution: 2.31→2.38 Å / % possible all: 99.8 |
Reflection | *PLUS Lowest resolution: 18 Å / Num. measured all: 708695 / Rmerge(I) obs: 0.086 |
Reflection shell | *PLUS % possible obs: 99.8 % / Rmerge(I) obs: 0.359 |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 2.31→18 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 18 Å / Rfactor Rfree: 0.2544 / Rfactor Rwork: 0.2225 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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