Literature summary for 3.1.3.1 extracted from

Arai, S.; Yonezawa, Y.; Ishibashi, M.; Matsumoto, F.; Adachi, M.; Tamada, T.; Tokunaga, H.; Blaber, M.; Tokunaga, M.; Kuroki, R.
Structural characteristics of alkaline phosphatase from the moderately halophilic bacterium Halomonas sp. 593 (2014), Acta Crystallogr. Sect. D, 70, 811-820.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Halomonas sp.

Crystallization (Commentary)

Crystallization (Comment)	Organism
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.

Crystallization (Comment)

Organism

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

Metals/Ions	Comment	Organism
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

Organism	UniProt	Comment	Textmining
Halomonas sp.	B5BP20	-	-