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Experimental Technique/Method:NEUTRON DIFFRACTION Resolution:1.5 Classification:HYDROLASE Release Date:2018-02-28 Deposition Date:2016-12-13 Revision Date: Molecular Weight:23588.62 Macromolecule Type:Protein Residue Count:223 Atom Site Count:1622 DOI:10.2210/pdb5mo2/pdb
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  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.68 Classification:TRANSFERASE Release Date:2018-02-28 Deposition Date:2017-11-27 Revision Date: Molecular Weight:74668.78 Macromolecule Type:Protein Residue Count:662 Atom Site Count:4684 DOI:10.2210/pdb6bq2/pdb Abstract: Polyamines are linear polycationic compounds that play a crucial role in the growth and development of higher plants. One triamine (spermidine, SPD) and two tetraamine isomers (spermine, SPM, and thermospermine, TSPM) are obtained by the transfer of the aminopropyl group from decarboxylated
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  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.99 Classification:LYASE Release Date:2018-02-28 Deposition Date:2017-02-21 Revision Date: Molecular Weight:52941.69 Macromolecule Type:Protein Residue Count:468 Atom Site Count:3452 DOI:10.2210/pdb5ux2/pdb
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  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.67 Classification:HYDROLASE/HYDROLASE inhibitor Release Date:2018-02-28 Deposition Date:2017-12-22 Revision Date: Molecular Weight:22341.11 Macromolecule Type:Protein Residue Count:198 Atom Site Count:1675 DOI:10.2210/pdb6bz2/pdb Abstract: We report here the design, synthesis, X-ray-structural, and biological studies of an exceptionally potent HIV-1 protease inhibitor 5. In this inhibitor, we incorporated an unprecedented structure-based designed 6-5-5-ring fused crown-like tetrahydropyranofuran as the P2-ligand, a cyclopropylaminobenzothiazole as the P2'-ligand and 3,5-difluorophenylmethyl as the P1-ligand. The resulting inhibitor 5, exhibited exceptional HIV-1 inhibitory and antiviral potency at picomolar level. Furthermore, it displayed antiviral IC50 values in picomolar range against a wide panel of highly multidrug-resistant HIV-1 variants. The inhibitor shows an extremely high genetic barrier against the emergence of drug-resistant variants. It also showed extremely potent dimerization inhibitory activity and penetrated CNS favourably. We have determined a high resolution X-ray structure of inhibitor 5-bound HIV-1 complex which provided molecular insight into the unprecedented activity profiles.
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.43 Classification:TRANSFERASE Release Date:2018-02-28 Deposition Date:2017-02-08 Revision Date: Molecular Weight:43561.48 Macromolecule Type:Protein Residue Count:372 Atom Site Count:3074 DOI:10.2210/pdb5n33/pdb
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  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.74 Classification:HYDROLASE Release Date:2018-02-28 Deposition Date:2018-01-29 Revision Date: Molecular Weight:155359.41 Macromolecule Type:Protein Residue Count:1332 Atom Site Count:10836 DOI:10.2210/pdb6ca3/pdb
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  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.04 Classification:VIRAL PROTEIN Release Date:2018-02-28 Deposition Date:2017-09-03 Revision Date: Molecular Weight:21381.66 Macromolecule Type:Protein Residue Count:177 Atom Site Count:1497 DOI:10.2210/pdb5yb3/pdb
Data Types:
  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.05 Classification:TRANSFERASE/ANTIBIOTIC Release Date:2018-02-28 Deposition Date:2017-10-20 Revision Date: Molecular Weight:33559.52 Macromolecule Type:Protein Residue Count:302 Atom Site Count:2127 DOI:10.2210/pdb6bc3/pdb
Data Types:
  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.15 Classification:OXIDOREDUCTASE Release Date:2018-02-28 Deposition Date:2017-06-29 Revision Date: Molecular Weight:105393.91 Macromolecule Type:Protein Residue Count:922 Atom Site Count:7113 DOI:10.2210/pdb5oc3/pdb Abstract: Amadoriases are a class of FAD-dependent enzymes that are found in fungi, yeast and bacteria and that are able to hydrolyze glycated amino acids, cleaving the sugar moiety from the amino acidic portion. So far, engineered Amadoriases have mostly found practical application in the measurement of the concentration of glycated albumin in blood samples. However, these engineered forms of Amadoriases show relatively low absolute activity and stability levels, which affect their conditions of use. Therefore, enzyme stabilization is desirable prior to function-altering molecular engineering. In this work, we describe a rational design strategy based on a computational screening method to evaluate a library of potentially stabilizing disulfide bonds. Our approach allowed the identification of two thermostable Amadoriase I mutants (SS03 and SS17) featuring a significantly higher T
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  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.0 Classification:HYDROLASE, LYASE/DNA Release Date:2018-02-28 Deposition Date:2017-07-31 Revision Date: Molecular Weight:75424.39 Macromolecule Type:Protein#DNA Residue Count:594 Atom Site Count:5354 DOI:10.2210/pdb5wn3/pdb Abstract: Human apurinic/apyrimidinic (AP) endonuclease 1 (APE1) is an essential DNA repair enzyme which uses a single active site to process DNA damage via two distinct activities: (1) AP-endonuclease and (2) 3' to 5' exonuclease. The AP-endonuclease activity cleaves at AP-sites, while the exonuclease activity excises bulkier 3' mismatches and DNA damage to generate clean DNA ends suitable for downstream repair. Molecular details of the exonuclease reaction and how one active site can accommodate various toxic DNA repair intermediates remains elusive despite being biologically important. Here, we report multiple high-resolution APE1-DNA structural snapshots revealing how APE1 removes 3' mismatches and DNA damage by placing the 3' group within the intra-helical DNA cavity via a non-base flipping mechanism. This process is facilitated by a DNA nick, instability of a mismatched/damaged base, and bending of the DNA. These results illustrate how APE1 cleanses DNA dirty-ends to generate suitable substrates for downstream repair enzymes.
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  • Tabular Data
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