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Open data
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Basic information
Entry | Database: PDB / ID: 7oxi | |||||||||
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Title | ttSlyD with W4A pseudo-wild-type S2 peptide | |||||||||
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![]() | ISOMERASE / FKBP / chaperone | |||||||||
Function / homology | ![]() peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / ribosomal small subunit assembly / protein refolding / cytosolic small ribosomal subunit / cytoplasmic translation / structural constituent of ribosome / zinc ion binding / metal ion binding / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Pazicky, S. / Lei, J. / Loew, C. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Impact of distant peptide substrate residues on enzymatic activity of SlyD. Authors: Pazicky, S. / Werle, A.A. / Lei, J. / Low, C. / Weininger, U. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 98 KB | Display | ![]() |
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PDB format | ![]() | 64 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 7oxgC ![]() 7oxhC ![]() 7oxjC ![]() 7oxkC ![]() 3cgmS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 17400.234 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 27634 / DSM 579 / HB8 / Gene: TTHA0346 / Production host: ![]() ![]() | ||||||
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#2: Protein/peptide | Mass: 1659.948 Da / Num. of mol.: 2 / Mutation: W23E, P25A, K28L, I30A / Source method: obtained synthetically / Source: (synth.) ![]() ![]() #3: Chemical | ChemComp-CL / | #4: Water | ChemComp-HOH / | Has ligand of interest | N | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.09 Å3/Da / Density % sol: 69.96 % |
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Crystal grow | Temperature: 292.15 K / Method: counter-diffusion / pH: 6.5 / Details: sodium cacodylate, MPD, PEG8000 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 14, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0332 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→41.86 Å / Num. obs: 10215 / % possible obs: 99.9 % / Redundancy: 18.5 % / Biso Wilson estimate: 95.41 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.0567 / Rpim(I) all: 0.0139 / Rrim(I) all: 0.05847 / Net I/σ(I): 30.51 |
Reflection shell | Resolution: 2.6→2.7 Å / Redundancy: 17.9 % / Rmerge(I) obs: 2.105 / Mean I/σ(I) obs: 1.43 / Num. unique obs: 988 / CC1/2: 0.704 / Rpim(I) all: 0.5057 / Rrim(I) all: 2.166 / % possible all: 99.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3cgm Resolution: 2.6→41.86 Å / SU ML: 0.3141 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 37.9729 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 119.85 Å2 | ||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→41.86 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: 16.4402406388 Å / Origin y: 57.0743859762 Å / Origin z: 38.7897743263 Å
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Refinement TLS group | Selection details: all |