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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.66 Classification:TRANSFERASE Release Date:2018-02-28 Deposition Date:2017-08-17 Revision Date: Molecular Weight:84968.47 Macromolecule Type:Protein Residue Count:704 Atom Site Count:5648 DOI:10.2210/pdb5os7/pdb
Data Types:
  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.85 Classification:OXYGEN TRANSPORT Release Date:2018-02-28 Deposition Date:2017-02-14 Revision Date: Molecular Weight:18683.97 Macromolecule Type:Protein Residue Count:154 Atom Site Count:1322 DOI:10.2210/pdb5ut7/pdb
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.9 Classification:TOXIN Release Date:2018-02-28 Deposition Date:2017-08-30 Revision Date: Molecular Weight:17191.67 Macromolecule Type:Protein Residue Count:152 Atom Site Count:1179 DOI:10.2210/pdb6au7/pdb
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  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.69 Classification:TRANSFERASE Release Date:2018-02-28 Deposition Date:2017-02-22 Revision Date: Molecular Weight:330199.81 Macromolecule Type:Protein Residue Count:2880 Atom Site Count:20647 DOI:10.2210/pdb5ux7/pdb
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Experimental Technique/Method:ELECTRON MICROSCOPY Resolution:7.5 Classification:DNA Release Date:2018-02-28 Deposition Date:2017-12-20 Revision Date: Molecular Weight:2715216.25 Macromolecule Type:DNA Residue Count:8803 Atom Site Count:180167 DOI:10.2210/pdb6by7/pdb Abstract: Building upon DNA origami technology, we introduce a method to reconstitute a single membrane protein into a self-assembled DNA nanobarrel that scaffolds a nanodisc-like lipid environment. Compared with the membrane-scaffolding-protein nanodisc technique, our approach gives rise to defined stoichiometry, controlled sizes, as well as enhanced stability and homogeneity in membrane protein reconstitution. We further demonstrate potential applications of the DNA nanobarrels in the structural analysis of membrane proteins.
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.4 Classification:MEMBRANE PROTEIN Release Date:2018-02-28 Deposition Date:2017-11-23 Revision Date: Molecular Weight:59222.86 Macromolecule Type:Protein Residue Count:516 Atom Site Count:4071 DOI:10.2210/pdb6f28/pdb Abstract: Starting from 1-4 and 7 structural templates, analogues based on bioisosteric replacements (5a-c vs 1, 2 and 6 vs 7) were synthesized for completing the SAR analysis. Interesting binding properties at GluA2, GluK1, and GluK3 receptors were discovered. The requirements for GluK3 interaction were elucidated by determining the X-ray structures of the GluK3-LBD with 2 and 5c and by computational studies. Antinociceptive potential was demonstrated for GluK1 partial agonist 3 and antagonist 7 (2 mg/kg ip).
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.89 Classification:OXIDOREDUCTASE Release Date:2018-02-28 Deposition Date:2017-05-19 Revision Date: Molecular Weight:124759.26 Macromolecule Type:Protein Residue Count:1156 Atom Site Count:8640 DOI:10.2210/pdb5o28/pdb Abstract: The natural product carolacton is a macrolide keto-carboxylic acid produced by the myxobacterium Sorangium cellulosum, and was originally described as an antibacterial compound. Here we show that carolacton targets FolD, a key enzyme from the folate-dependent C1 metabolism. We characterize the interaction between bacterial FolD and carolacton biophysically, structurally and biochemically. Carolacton binds FolD with nanomolar affinity, and the crystal structure of the FolD-carolacton complex reveals the mode of binding. We show that the human FolD orthologs, MTHFD1 and MTHFD2, are also inhibited in the low nM range, and that micromolar concentrations of carolacton inhibit the growth of cancer cell lines. As mitochondrial MTHFD2 is known to be upregulated in cancer cells, it may be possible to use carolacton as an inhibitor tool compound to assess MTHFD2 as an anti-cancer target.
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.8 Classification:SPLICING Release Date:2018-02-28 Deposition Date:2016-10-28 Revision Date: Molecular Weight:31145.56 Macromolecule Type:Protein Residue Count:272 Atom Site Count:1942 DOI:10.2210/pdb5m88/pdb
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  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.55 Classification:HYDROLASE Release Date:2018-02-28 Deposition Date:2018-02-11 Revision Date: Molecular Weight:12322.06 Macromolecule Type:Protein Residue Count:107 Atom Site Count:817 DOI:10.2210/pdb6ce8/pdb
Data Types:
  • Tabular Data
Experimental Technique/Method:SOLUTION NMR Resolution: Classification:MEMBRANE PROTEIN Release Date:2018-02-28 Deposition Date:2017-03-13 Revision Date: Molecular Weight:40776.99 Macromolecule Type:Protein Residue Count:348 Atom Site Count:2588 DOI:10.2210/pdb5nf8/pdb
Data Types:
  • Tabular Data
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