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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.1 Classification:LYASE Release Date:2018-02-28 Deposition Date:2017-06-01 Revision Date: Molecular Weight:343175.16 Macromolecule Type:Protein Residue Count:3114 Atom Site Count:21803 DOI:10.2210/pdb5o5c/pdb Abstract: The Gram-negative bacterium Erwinia amylovora is the etiological agent of fire blight, a devastating disease which affects Rosaceae such as apple, pear and quince. The siderophore desferrioxamine E plays an important role in bacterial pathogenesis by scavenging iron from the host. DfoJ, DfoA and DfoC are the enzymes responsible for desferrioxamine production starting from lysine. We have determined the crystal structures of each enzyme in the desferrioxamine E pathway and demonstrate that the biosynthesis involves the concerted action of DfoJ, followed by DfoA and lastly DfoC. These data provide the first crystal structures of a Group II pyridoxal-dependent lysine decarboxylase, a cadaverine monooxygenase and a desferrioxamine synthetase. DfoJ is a homodimer made up of three domains. Each monomer contributes to the completion of the active site, which is positioned at the dimer interface. DfoA is the first structure of a cadaverine monooxygenase. It forms homotetramers whose subunits are built by two domains: one for FAD and one for NADP
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.3 Classification:SPLICING Release Date:2018-02-28 Deposition Date:2016-10-28 Revision Date: Molecular Weight:81377.37 Macromolecule Type:Protein Residue Count:720 Atom Site Count:5519 DOI:10.2210/pdb5m8c/pdb
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  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION, NEUTRON DIFFRACTION Resolution:1.8 Classification:lyase/lyase inhibitor Release Date:2018-02-28 Deposition Date:2017-10-20 Revision Date: Molecular Weight:29612.79 Macromolecule Type:Protein Residue Count:260 Atom Site Count:2066 DOI:10.2210/pdb6bcc/pdb Abstract: Human carbonic anhydrases (hCAs) play various roles in cells, and have been drug targets for decades. Sequence similarities of hCA isoforms necessitate designing specific inhibitors, which requires detailed structural information for hCA-inhibitor complexes. We present room temperature neutron structures of hCA II in complex with three clinical drugs that provide in-depth analysis of drug binding, including protonation states of the inhibitors, hydration water structure, and direct visualization of hydrogen-bonding networks in the enzyme's active site. All sulfonamide inhibitors studied bind to the Zn metal center in the deprotonated, anionic, form. Other chemical groups of the drugs can remain neutral or be protonated when bound to hCA II. MD simulations have shown that flexible functional groups of the inhibitors may alter their conformations at room temperature and occupy different sub-sites. This study offers insights into the design of specific drugs to target cancer-related hCA isoform IX.
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.48 Classification:STRUCTURAL PROTEIN Release Date:2018-02-28 Deposition Date:2017-03-22 Revision Date: Molecular Weight:104758.02 Macromolecule Type:Protein Residue Count:952 Atom Site Count:7018 DOI:10.2210/pdb5xcc/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:12361.07 Macromolecule Type:Protein Residue Count:107 Atom Site Count:819 DOI:10.2210/pdb6cec/pdb
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.8 Classification:OXYGEN TRANSPORT Release Date:2018-02-28 Deposition Date:2017-02-14 Revision Date: Molecular Weight:18475.99 Macromolecule Type:Protein Residue Count:154 Atom Site Count:1284 DOI:10.2210/pdb5utc/pdb
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  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.46 Classification:METAL BINDING PROTEIN Release Date:2018-02-28 Deposition Date:2017-08-31 Revision Date: Molecular Weight:17506.45 Macromolecule Type:Protein Residue Count:159 Atom Site Count:978 DOI:10.2210/pdb6auc/pdb Abstract: Artificial metalloproteins (ArMs) containing Co
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.88 Classification:TOXIN Release Date:2018-02-28 Deposition Date:2017-09-01 Revision Date: Molecular Weight:4344.14 Macromolecule Type:Protein Residue Count:39 Atom Site Count:272 DOI:10.2210/pdb6avc/pdb
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  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.61 Classification:TRANSFERASE Release Date:2018-02-28 Deposition Date:2017-02-06 Revision Date: Molecular Weight:43651.64 Macromolecule Type:Protein Residue Count:372 Atom Site Count:3135 DOI:10.2210/pdb5n1d/pdb
Data Types:
  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.77 Classification:TRANSFERASE Release Date:2018-02-28 Deposition Date:2017-02-08 Revision Date: Molecular Weight:43494.39 Macromolecule Type:Protein Residue Count:372 Atom Site Count:2956 DOI:10.2210/pdb5n3d/pdb
Data Types:
  • Tabular Data
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