Sodium in PDB 2x98: H.Salinarum Alkaline Phosphatase

All present enzymatic activity of H.Salinarum Alkaline Phosphatase:
3.1.3.1;

The structure of H.Salinarum Alkaline Phosphatase, PDB code: 2x98 was solved by A.Wende, P.Johansson, M.Grininger, D.Oesterhelt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 1.70
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	72.143, 152.524, 86.799, 90.00, 110.00, 90.00
R / Rfree (%)	16.042 / 19.771

The structure of H.Salinarum Alkaline Phosphatase also contains other interesting chemical elements:

Magnesium	(Mg)	11 atoms
Zinc	(Zn)	4 atoms
Chlorine	(Cl)	13 atoms

The binding sites of Sodium atom in the H.Salinarum Alkaline Phosphatase (pdb code 2x98). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the H.Salinarum Alkaline Phosphatase, PDB code: 2x98:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the H.Salinarum Alkaline Phosphatase


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of H.Salinarum Alkaline Phosphatase within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1482 b:8.0 occ:0.50 O A:ARG98 2.2 4.2 1.0 OD1 A:ASP453 2.2 7.8 1.0 CG A:ASP453 3.1 9.5 1.0 C A:ARG98 3.3 4.3 1.0 CA A:ASP453 3.5 6.8 1.0 CB A:ASP453 3.6 7.5 1.0 N A:ARG98 3.7 4.7 1.0 CG A:ARG98 3.9 7.1 1.0 CA A:ARG98 4.0 4.4 1.0 CD A:ARG98 4.1 8.5 1.0 OD2 A:ASP453 4.1 6.9 1.0 C A:ASP453 4.3 7.2 1.0 N A:GLY99 4.4 3.0 1.0 CB A:ARG98 4.6 3.3 1.0 CA A:GLY99 4.7 4.2 1.0 N A:ASP453 4.7 8.1 1.0 O A:PHE452 4.7 8.2 1.0 O A:ASP453 4.9 7.7 1.0 C A:SER97 4.9 6.2 1.0 N A:ALA454 4.9 6.9 1.0

Sodium binding site 2 out of 2 in the H.Salinarum Alkaline Phosphatase


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of H.Salinarum Alkaline Phosphatase within 5.0Å range: probe atom residue distance (Å) B Occ B:Na1483 b:9.7 occ:0.50 O B:ARG98 2.1 5.8 1.0 OD1 B:ASP453 2.2 7.8 1.0 CG B:ASP453 3.1 8.6 1.0 C B:ARG98 3.3 6.3 1.0 CA B:ASP453 3.5 6.8 1.0 CB B:ASP453 3.6 6.8 1.0 N B:ARG98 3.6 5.9 1.0 CG B:ARG98 3.8 10.7 1.0 CA B:ARG98 4.0 6.0 1.0 CD B:ARG98 4.1 10.0 1.0 OD2 B:ASP453 4.1 6.8 1.0 C B:ASP453 4.3 7.5 1.0 N B:GLY99 4.4 5.8 1.0 CB B:ARG98 4.5 4.9 1.0 CA B:GLY99 4.6 7.0 1.0 N B:ASP453 4.6 6.6 1.0 O B:PHE452 4.7 7.8 1.0 O B:ASP453 4.8 8.3 1.0 C B:SER97 4.8 7.4 1.0 N B:ALA454 4.8 8.8 1.0

A.Wende, P.Johansson, R.Vollrath, M.Dyall-Smith, D.Oesterhelt, M.Grininger. Structural and Biochemical Characterization of A Halophilic Archaeal Alkaline Phosphatase. J.Mol.Biol. V. 400 52 2010.
ISSN: ISSN 0022-2836
PubMed: 20438737
DOI: 10.1016/J.JMB.2010.04.057