Magnesium in PDB 6pd0: Crystal Structure of the Bacterial Cellulose Synthase Subunit G (Bcsg) From Escherichia Coli, Catalytic Domain

The structure of Crystal Structure of the Bacterial Cellulose Synthase Subunit G (Bcsg) From Escherichia Coli, Catalytic Domain, PDB code: 6pd0 was solved by A.C.Anderson, T.Brenner, J.T.Weadge, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.96 / 1.75
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.510, 76.920, 95.920, 90.00, 90.58, 90.00
R / Rfree (%)	16.1 / 19.9

The structure of Crystal Structure of the Bacterial Cellulose Synthase Subunit G (Bcsg) From Escherichia Coli, Catalytic Domain also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of the Bacterial Cellulose Synthase Subunit G (Bcsg) From Escherichia Coli, Catalytic Domain (pdb code 6pd0). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Bacterial Cellulose Synthase Subunit G (Bcsg) From Escherichia Coli, Catalytic Domain, PDB code: 6pd0:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the Bacterial Cellulose Synthase Subunit G (Bcsg) From Escherichia Coli, Catalytic Domain


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Bacterial Cellulose Synthase Subunit G (Bcsg) From Escherichia Coli, Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:12.1 occ:0.91 O A:ASN383 2.0 12.8 1.0 O A:HOH870 2.0 13.5 1.0 O A:HOH790 2.0 14.6 1.0 O A:HOH867 2.1 12.2 1.0 O A:THR378 2.1 15.0 1.0 OD1 A:ASP381 2.2 15.3 1.0 CG A:ASP381 3.1 15.8 1.0 C A:ASN383 3.2 15.3 1.0 C A:THR378 3.3 13.4 1.0 OD2 A:ASP381 3.5 14.1 1.0 N A:ASN383 3.8 14.7 1.0 CA A:ASN383 4.0 13.2 1.0 OE2 A:GLU236 4.1 16.4 1.0 O A:HOH1163 4.1 32.3 1.0 CA A:THR378 4.2 12.9 1.0 N A:SER384 4.2 14.7 1.0 N A:GLU379 4.2 14.8 1.0 CA A:GLU379 4.3 14.5 1.0 O A:HOH1094 4.3 25.9 1.0 O A:GLU379 4.3 17.9 1.0 C A:GLU379 4.3 16.7 1.0 N A:ASP381 4.3 14.9 1.0 CA A:SER384 4.4 19.9 1.0 OE1 A:GLU236 4.4 14.5 1.0 CB A:ASP381 4.4 15.6 1.0 CB A:ASN383 4.5 11.3 1.0 CB A:THR378 4.6 14.6 1.0 N A:LYS382 4.6 17.2 1.0 C A:SER384 4.6 19.0 1.0 CD A:GLU236 4.7 14.3 1.0 C A:ASP381 4.7 16.1 1.0 CA A:ASP381 4.7 14.3 1.0 O A:HOH1174 4.7 41.7 1.0 N A:ARG385 4.8 13.1 1.0 N A:LYS380 4.9 14.8 1.0 C A:LYS382 4.9 19.8 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the Bacterial Cellulose Synthase Subunit G (Bcsg) From Escherichia Coli, Catalytic Domain


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Bacterial Cellulose Synthase Subunit G (Bcsg) From Escherichia Coli, Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:14.6 occ:0.96 O B:ASN383 2.0 17.4 1.0 O B:HOH807 2.0 14.3 1.0 O B:THR378 2.0 15.0 1.0 O B:HOH733 2.0 18.0 1.0 O B:HOH798 2.1 16.0 1.0 OD1 B:ASP381 2.1 16.5 1.0 CG B:ASP381 3.1 17.3 1.0 C B:ASN383 3.2 15.9 1.0 C B:THR378 3.2 14.8 1.0 OD2 B:ASP381 3.4 15.2 1.0 N B:ASN383 3.7 15.4 1.0 CA B:ASN383 3.9 15.8 1.0 OE2 B:GLU236 4.0 18.5 1.0 CA B:THR378 4.0 15.0 1.0 N B:GLU379 4.1 14.4 1.0 N B:SER384 4.2 19.6 1.0 O B:HOH1035 4.2 29.3 1.0 CA B:GLU379 4.2 18.9 1.0 O B:GLU379 4.3 20.7 1.0 C B:GLU379 4.3 21.5 1.0 N B:ASP381 4.3 13.6 1.0 O B:HOH1084 4.3 30.0 1.0 CB B:ASP381 4.4 15.9 1.0 OE1 B:GLU236 4.4 18.2 1.0 CB B:ASN383 4.4 17.2 1.0 CA B:SER384 4.4 22.4 1.0 CB B:THR378 4.4 11.5 1.0 CA B:ASP381 4.6 15.1 1.0 N B:LYS382 4.6 14.9 1.0 C B:ASP381 4.6 15.0 1.0 CD B:GLU236 4.6 16.2 1.0 C B:SER384 4.7 16.3 1.0 N B:LYS380 4.9 15.3 1.0 C B:LYS382 4.9 20.2 1.0 N B:ARG385 4.9 17.1 1.0

A.C.Anderson, T.Brenner, J.T.Weadge. Crystal Structure of the Bacterial Cellulose Synthase Subunit G (Bcsg) From Escherichia Coli, Catalytic Domain To Be Published.