Sodium in PDB 8hwk: Limosilactobacillus Reuteri N1 Gtfb-Maltohexaose

All present enzymatic activity of Limosilactobacillus Reuteri N1 Gtfb-Maltohexaose:
2.4.1.5;

The structure of Limosilactobacillus Reuteri N1 Gtfb-Maltohexaose, PDB code: 8hwk was solved by J.J.Dong, Y.X.Bai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.74 / 2.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	206.15, 101.188, 106.791, 90, 108.84, 90
R / Rfree (%)	21.5 / 26.1

The binding sites of Sodium atom in the Limosilactobacillus Reuteri N1 Gtfb-Maltohexaose (pdb code 8hwk). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Limosilactobacillus Reuteri N1 Gtfb-Maltohexaose, PDB code: 8hwk:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Limosilactobacillus Reuteri N1 Gtfb-Maltohexaose


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Limosilactobacillus Reuteri N1 Gtfb-Maltohexaose within 5.0Å range: probe atom residue distance (Å) B Occ A:Na901 b:16.4 occ:1.00 O A:HIS265 2.2 16.1 1.0 OD1 A:ASP221 2.2 17.2 1.0 OD1 A:ASN721 2.3 15.8 1.0 OE2 A:GLU215 2.3 15.8 1.0 O A:GLU215 2.4 21.5 1.0 CG A:ASP221 3.1 17.9 1.0 CD A:GLU215 3.3 16.2 1.0 OD2 A:ASP221 3.3 17.8 1.0 CG A:ASN721 3.4 16.2 1.0 C A:HIS265 3.4 17.9 1.0 C A:GLU215 3.5 20.3 1.0 CG A:GLU215 4.0 17.7 1.0 CA A:GLU215 4.1 19.6 1.0 ND2 A:ASN721 4.1 16.5 1.0 CG2 A:ILE266 4.1 16.8 1.0 O A:ASN721 4.2 18.1 1.0 OE1 A:GLU215 4.2 15.4 1.0 N A:ILE266 4.2 17.1 1.0 CA A:ILE266 4.3 16.3 1.0 CB A:HIS265 4.3 19.6 1.0 CA A:HIS265 4.4 19.4 1.0 O A:HOH1027 4.5 4.2 1.0 CB A:ASN721 4.5 16.7 1.0 CB A:ASP221 4.6 18.2 1.0 O A:ILE222 4.6 16.0 1.0 CA A:ASN721 4.6 18.0 1.0 CB A:GLU215 4.6 18.4 1.0 N A:PHE216 4.6 20.2 1.0 C A:ASN721 4.8 18.5 1.0 CB A:ILE266 4.9 16.4 1.0 CA A:PHE216 4.9 19.9 1.0

Sodium binding site 2 out of 2 in the Limosilactobacillus Reuteri N1 Gtfb-Maltohexaose


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Limosilactobacillus Reuteri N1 Gtfb-Maltohexaose within 5.0Å range: probe atom residue distance (Å) B Occ B:Na901 b:15.3 occ:1.00 OD1 B:ASN721 2.2 15.1 1.0 O B:GLU215 2.2 17.4 1.0 O B:HIS265 2.2 15.5 1.0 OD1 B:ASP221 2.2 15.4 1.0 O B:HOH1035 2.2 14.4 1.0 OE2 B:GLU215 2.5 15.8 1.0 CG B:ASP221 3.2 16.4 1.0 CG B:ASN721 3.3 15.5 1.0 C B:GLU215 3.4 18.3 1.0 C B:HIS265 3.4 16.7 1.0 OD2 B:ASP221 3.4 15.8 1.0 CD B:GLU215 3.5 16.1 1.0 ND2 B:ASN721 4.0 15.3 1.0 CG B:GLU215 4.0 16.8 1.0 CA B:GLU215 4.0 17.6 1.0 CG2 B:ILE266 4.2 16.0 1.0 CB B:HIS265 4.2 18.3 1.0 N B:ILE266 4.3 16.1 1.0 O B:ASN721 4.3 15.7 1.0 CA B:HIS265 4.3 17.9 1.0 O B:HOH1041 4.4 11.0 1.0 OE1 B:GLU215 4.4 15.6 1.0 CA B:ILE266 4.4 15.8 1.0 CB B:ASN721 4.4 15.9 1.0 N B:PHE216 4.5 19.3 1.0 CB B:ASP221 4.6 17.1 1.0 CB B:GLU215 4.6 17.2 1.0 CA B:ASN721 4.6 16.6 1.0 CA B:PHE216 4.7 19.9 1.0 O B:ILE222 4.8 16.1 1.0 C B:ASN721 4.9 16.8 1.0 CB B:ILE266 5.0 16.0 1.0

J.J.Dong, Y.X.Bai. The Evolutionary Advantage of A Tunnel Structure at Donor Subsites on the Processive Mechanism To Be Published.