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Open data
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Basic information
Entry | Database: PDB / ID: 7msk | ||||||
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Title | ThuS glycosin S-glycosyltransferase | ||||||
![]() | Glyco_trans_2-like domain-containing protein | ||||||
![]() | BIOSYNTHETIC PROTEIN / glycosin / RiPP / glycosyltransferase | ||||||
Function / homology | protein S-linked glycosylation via cysteine / Peptide S-glycosyltransferase, SunS family / Glycosyltransferase 2-like / Glycosyl transferase family 2 / Nucleotide-diphospho-sugar transferases / Chem-U2F / Glyco_trans_2-like domain-containing protein![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Garg, N. / Nair, S.K. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structural and mechanistic investigations of protein S-glycosyltransferases. Authors: Fujinami, D. / Garcia de Gonzalo, C.V. / Biswas, S. / Hao, Y. / Wang, H. / Garg, N. / Lukk, T. / Nair, S.K. / van der Donk, W.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 195 KB | Display | ![]() |
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PDB format | ![]() | 152.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.3 MB | Display | ![]() |
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Full document | ![]() | 1.3 MB | Display | |
Data in XML | ![]() | 34.4 KB | Display | |
Data in CIF | ![]() | 48.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7msnC ![]() 7mspC C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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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: 50454.461 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: bthur0009_56280 / Production host: ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.51 Å3/Da / Density % sol: 51.04 % |
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Crystal grow | Temperature: 283 K / Method: vapor diffusion, hanging drop Details: 15% PEG 3350 200 mM ammonium nitrate 100 mM BisTris HCl pH=6.5 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Dec 19, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9786 Å / Relative weight: 1 |
Reflection | Resolution: 2.06→90.3 Å / Num. obs: 61544 / % possible obs: 99.7 % / Redundancy: 6.3 % / CC1/2: 0.999 / Net I/σ(I): 16.9 |
Reflection shell | Resolution: 2.06→2.09 Å / Num. unique obs: 3042 / CC1/2: 0.831 |
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Processing
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Refinement | Method to determine structure: ![]() Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 113.68 Å2 / Biso mean: 41.5 Å2 / Biso min: 19.11 Å2
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Refinement step | Cycle: final / Resolution: 2.06→25 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.06→2.113 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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