Sodium in PDB 8ewt: Bile Salt Hydrolase A From Lactobacillus Gasseri Bound to Covalent Probe

The structure of Bile Salt Hydrolase A From Lactobacillus Gasseri Bound to Covalent Probe, PDB code: 8ewt was solved by M.E.Walker, M.R.Redinbo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.22 / 2.03
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	108.44, 108.44, 161.518, 90, 90, 90
R / Rfree (%)	18.6 / 22.6

The binding sites of Sodium atom in the Bile Salt Hydrolase A From Lactobacillus Gasseri Bound to Covalent Probe (pdb code 8ewt). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Bile Salt Hydrolase A From Lactobacillus Gasseri Bound to Covalent Probe, PDB code: 8ewt:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Bile Salt Hydrolase A From Lactobacillus Gasseri Bound to Covalent Probe


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Bile Salt Hydrolase A From Lactobacillus Gasseri Bound to Covalent Probe within 5.0Å range: probe atom residue distance (Å) B Occ A:Na402 b:59.2 occ:1.00 O A:TYR41 2.4 52.4 1.0 O A:HOH568 2.5 59.8 1.0 OD1 A:ASN46 2.5 57.3 1.0 O A:HOH563 2.6 53.5 1.0 O A:LEU44 2.7 57.4 1.0 CG A:ASN46 3.6 54.9 1.0 C A:TYR41 3.6 51.2 1.0 C A:LEU44 3.9 54.2 1.0 O A:LYS42 3.9 55.5 1.0 ND2 A:ASN46 4.1 57.5 1.0 C A:LYS42 4.1 50.7 1.0 N A:LEU44 4.3 52.7 1.0 N A:ASN46 4.3 54.4 1.0 N A:TYR41 4.4 54.3 1.0 CA A:TYR41 4.5 52.1 1.0 N A:LYS42 4.6 49.5 1.0 CA A:LYS42 4.6 48.5 1.0 N A:PHE43 4.6 52.1 1.0 CA A:LEU44 4.7 52.3 1.0 N A:ASP45 4.8 54.8 1.0 CA A:ASP45 4.8 54.7 1.0 CB A:TYR41 4.8 51.8 1.0 C A:ASP45 4.8 56.5 1.0 CB A:ASN46 4.8 49.9 1.0 CA A:ASN46 5.0 51.5 1.0 C A:PHE43 5.0 50.3 1.0

Sodium binding site 2 out of 2 in the Bile Salt Hydrolase A From Lactobacillus Gasseri Bound to Covalent Probe


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Bile Salt Hydrolase A From Lactobacillus Gasseri Bound to Covalent Probe within 5.0Å range: probe atom residue distance (Å) B Occ B:Na402 b:50.0 occ:1.00 OD1 B:ASN46 2.3 48.2 1.0 O B:HOH586 2.4 50.5 1.0 O B:HOH583 2.4 56.5 1.0 O B:LEU44 2.4 47.5 1.0 O B:HOH580 2.5 51.4 1.0 O B:TYR41 2.6 50.2 1.0 CG B:ASN46 3.3 46.6 1.0 C B:LEU44 3.6 47.1 1.0 C B:TYR41 3.7 45.4 1.0 N B:ASN46 3.7 46.8 1.0 ND2 B:ASN46 4.0 50.5 1.0 C B:ASP45 4.2 46.8 1.0 O B:HOH590 4.2 56.3 1.0 N B:TYR41 4.2 43.8 1.0 CA B:ASP45 4.3 47.6 1.0 CA B:TYR41 4.4 44.9 1.0 N B:LEU44 4.4 46.1 1.0 N B:ASP45 4.4 46.0 1.0 CB B:ASN46 4.4 42.5 1.0 CA B:ASN46 4.4 43.8 1.0 O B:LYS42 4.5 42.7 1.0 C B:LYS42 4.5 45.1 1.0 CB B:TYR41 4.6 43.9 1.0 CA B:LEU44 4.7 45.6 1.0 N B:LYS42 4.7 43.5 1.0 N B:PHE43 4.9 39.5 1.0 CA B:LYS42 4.9 43.3 1.0 O B:ASP45 4.9 50.2 1.0

M.E.Walker, M.R.Redinbo. Structural Diversity of Bile Salt Hydrolases Reveals Rationale For Substrate Selectivity To Be Published.