Cloned (Comment) | Organism |
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expression in Escherichia coli | Halomonas sp. |
Crystallization (Comment) | Organism |
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to 2.1 A resolution. The unit cell contains one dimer unit corresponding to the biological unit. The surface of the dimer is substantially more acidic than that of the Vibrio sp. G15-21 alkaline phosphatase dimer, and may enable the solubility of Halomonas sp. alkaline phosphatase under high-salt conditions. The monomer unit of Halomonas sp. alkaline phosphatase forms a substantially larger hydrophobic interior comprising 329 C atoms from completely buried residues compared with Vibrio sp. G15-21 alkaline phosphatase | Halomonas sp. |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | metal-binding site M3, consisting of residues Asp12, Thr118 and Glu264. Metal-binding site M5 site is composed of at least five chelating O atoms, from the main chain of Gly103, O1 of Asp255 and O2 of Asp257 and two O atoms from water molecules, weakly chelating Mg2+ | Halomonas sp. | |
additional information | metal-binding site M4 site is composed of six O atoms from the main chains of Ala45, Lys46, Gly48 and Ser481, the O atom of Ser482 and one water O atom, chelating a metal ion with distances of 2.2-2.7 A | Halomonas sp. | |
Zn2+ | metal-binding site M1 site consists of residues Asp269, His273 and His461, in which Zn2+ is chelated by three O and two N atoms with distances of 2.12.5 A. In the metal-binding site M2 residues Asp12, Ser65, Asp311 and His312 Zn2+ is chelated by five O atoms and one N atom with distances of 2.0-2.1 A | Halomonas sp. |
Organism | UniProt | Comment | Textmining |
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Halomonas sp. | B5BP20 | - |
- |