Magnesium in PDB 5xg3: Crystal Structure of the Atpgs-Engaged Smc Head Domain with An Extended Coiled Coil Bound to the C-Terminal Domain of Scpa Derived From Bacillus Subtilis

The structure of Crystal Structure of the Atpgs-Engaged Smc Head Domain with An Extended Coiled Coil Bound to the C-Terminal Domain of Scpa Derived From Bacillus Subtilis, PDB code: 5xg3 was solved by H.-C.Shin, H.Lee, B.-H.Oh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.99 / 3.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	88.103, 104.783, 185.220, 90.00, 90.00, 90.00
R / Rfree (%)	26.1 / 29.6

The structure of Crystal Structure of the Atpgs-Engaged Smc Head Domain with An Extended Coiled Coil Bound to the C-Terminal Domain of Scpa Derived From Bacillus Subtilis also contains other interesting chemical elements:

Cobalt

(Co)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of the Atpgs-Engaged Smc Head Domain with An Extended Coiled Coil Bound to the C-Terminal Domain of Scpa Derived From Bacillus Subtilis (pdb code 5xg3). 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 Atpgs-Engaged Smc Head Domain with An Extended Coiled Coil Bound to the C-Terminal Domain of Scpa Derived From Bacillus Subtilis, PDB code: 5xg3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the Atpgs-Engaged Smc Head Domain with An Extended Coiled Coil Bound to the C-Terminal Domain of Scpa Derived From Bacillus Subtilis


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 Atpgs-Engaged Smc Head Domain with An Extended Coiled Coil Bound to the C-Terminal Domain of Scpa Derived From Bacillus Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1202 b:17.4 occ:1.00 OE1 A:GLN143 2.0 32.3 1.0 O3G A:AGS1201 2.7 50.4 1.0 CD A:GLN143 2.7 38.5 1.0 S1G A:AGS1201 2.9 26.9 1.0 O1B A:AGS1201 2.9 34.6 1.0 CB A:SER38 3.3 35.3 1.0 NE2 A:GLN1118 3.3 58.7 1.0 PG A:AGS1201 3.3 37.5 1.0 CG A:GLN143 3.4 38.0 1.0 OD1 A:ASP1117 3.6 45.9 1.0 O2B A:AGS1201 3.6 37.4 1.0 NE2 A:GLN143 3.6 48.8 1.0 PB A:AGS1201 3.7 42.9 1.0 OD2 A:ASP1117 3.7 22.1 1.0 O3B A:AGS1201 3.9 38.9 1.0 CG A:ASP1117 4.0 31.5 1.0 N A:SER38 4.1 19.4 1.0 CA A:SER38 4.1 21.6 1.0 OG A:SER38 4.2 29.6 1.0 CD A:GLN1118 4.4 50.0 1.0 O2G A:AGS1201 4.6 40.4 1.0 N B:GLY1091 4.6 24.3 1.0 CA B:GLY1091 4.8 38.5 1.0 CB A:GLN143 4.9 40.6 1.0 OE1 A:GLN1118 5.0 30.2 1.0 NZ A:LYS37 5.0 51.8 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the Atpgs-Engaged Smc Head Domain with An Extended Coiled Coil Bound to the C-Terminal Domain of Scpa Derived From Bacillus Subtilis


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 Atpgs-Engaged Smc Head Domain with An Extended Coiled Coil Bound to the C-Terminal Domain of Scpa Derived From Bacillus Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1202 b:37.3 occ:1.00 OE1 B:GLN143 2.4 43.9 1.0 S1G B:AGS1201 2.4 41.6 1.0 NE2 B:GLN143 2.6 35.6 1.0 CD B:GLN143 2.8 34.5 1.0 O1B B:AGS1201 2.8 28.4 1.0 CB B:SER38 3.0 36.4 1.0 O B:HOH1302 3.4 38.9 1.0 O B:HOH1303 3.4 19.5 1.0 OG B:SER38 3.5 46.1 1.0 PG B:AGS1201 3.7 73.3 1.0 O3G B:AGS1201 3.9 67.3 1.0 PB B:AGS1201 3.9 28.8 1.0 CG B:GLN143 4.2 34.8 1.0 O3B B:AGS1201 4.2 36.9 1.0 O2B B:AGS1201 4.4 52.0 1.0 OG A:SER1090 4.4 19.6 1.0 N A:GLY1091 4.4 23.7 1.0 CA B:SER38 4.4 32.2 1.0 N B:SER38 4.6 38.6 1.0 CA A:GLY1091 4.7 22.0 1.0 CG B:GLN1118 4.7 44.5 1.0 CB B:GLN143 4.9 40.5 1.0 O2G B:AGS1201 4.9 58.2 1.0 CG2 B:ILE1147 4.9 30.4 1.0

M.L.Diebold-Durand, H.Lee, L.B.Ruiz Avila, H.Noh, H.C.Shin, H.Im, F.P.Bock, F.Burmann, A.Durand, A.Basfeld, S.Ham, J.Basquin, B.-H.Oh, S.Gruber. Structure of Full-Length Smc and Rearrangements Required For Chromosome Organization Mol. Cell V. 67 334 2017.
ISSN: ISSN 1097-4164
PubMed: 28689660
DOI: 10.1016/J.MOLCEL.2017.06.010