6F52
 
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6F4W
 | | Crystal structure of H. pylori purine nucleoside phosphorylase in complex with formycin A | | Descriptor: | (1S)-1-(7-amino-1H-pyrazolo[4,3-d]pyrimidin-3-yl)-1,4-anhydro-D-ribitol, Purine nucleoside phosphorylase DeoD-type | | Authors: | Stefanic, Z. | | Deposit date: | 2017-11-30 | | Release date: | 2018-02-14 | | Last modified: | 2024-01-17 | | Method: | X-RAY DIFFRACTION (2.293 Å) | | Cite: | Helicobacter pylori purine nucleoside phosphorylase shows new distribution patterns of open and closed active site conformations and unusual biochemical features.
FEBS J., 285, 2018
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6F5I
 | | Crystal structure of H. pylori purine nucleoside phosphorylase | | Descriptor: | METHANOL, Purine nucleoside phosphorylase DeoD-type | | Authors: | Stefanic, Z. | | Deposit date: | 2017-12-01 | | Release date: | 2018-02-14 | | Last modified: | 2024-01-17 | | Method: | X-RAY DIFFRACTION (2.298 Å) | | Cite: | Helicobacter pylori purine nucleoside phosphorylase shows new distribution patterns of open and closed active site conformations and unusual biochemical features.
FEBS J., 285, 2018
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6F5A
 | | Crystal structure of H. pylori purine nucleoside phosphorylase | | Descriptor: | Purine nucleoside phosphorylase DeoD-type | | Authors: | Stefanic, Z. | | Deposit date: | 2017-12-01 | | Release date: | 2018-02-14 | | Last modified: | 2024-11-13 | | Method: | X-RAY DIFFRACTION (2.201 Å) | | Cite: | Helicobacter pylori purine nucleoside phosphorylase shows new distribution patterns of open and closed active site conformations and unusual biochemical features.
FEBS J., 285, 2018
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6F4X
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5LU0
 | | Crystal structure of H. pylori referent strain in complex with PO4 | | Descriptor: | 1,2-ETHANEDIOL, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, PHOSPHATE ION, ... | | Authors: | Stefanic, Z. | | Deposit date: | 2016-09-07 | | Release date: | 2017-09-20 | | Last modified: | 2024-05-01 | | Method: | X-RAY DIFFRACTION (1.73 Å) | | Cite: | Helicobacter pylori purine nucleoside phosphorylase shows new distribution patterns of open and closed active site conformations and unusual biochemical features.
FEBS J., 285, 2018
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