Magnesium in PDB 6rvm: Cell Division Protein Ftsz From Staphylococcus Aureus, Apo Form

Protein crystallography data

The structure of Cell Division Protein Ftsz From Staphylococcus Aureus, Apo Form, PDB code: 6rvm was solved by C.Fernandez-Tornero, J.M.Andreu, A.J.Canosa-Valls, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.16 / 2.16
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 72.564, 78.805, 225.639, 90.00, 90.00, 90.00
R / Rfree (%) 23 / 25.6

Other elements in 6rvm:

The structure of Cell Division Protein Ftsz From Staphylococcus Aureus, Apo Form also contains other interesting chemical elements:

Chlorine (Cl) 9 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cell Division Protein Ftsz From Staphylococcus Aureus, Apo Form (pdb code 6rvm). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Cell Division Protein Ftsz From Staphylococcus Aureus, Apo Form, PDB code: 6rvm:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 6rvm

Go back to Magnesium Binding Sites List in 6rvm
Magnesium binding site 1 out of 2 in the Cell Division Protein Ftsz From Staphylococcus Aureus, Apo Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cell Division Protein Ftsz From Staphylococcus Aureus, Apo Form within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg407

b:67.2
occ:1.00
O C:GLY107 2.4 80.2 1.0
H C:GLY21 2.5 73.4 1.0
H C:GLY110 2.6 71.7 1.0
N C:GLY21 3.2 61.1 1.0
HA3 C:GLY110 3.3 68.1 1.0
H C:GLY22 3.4 72.0 1.0
N C:GLY110 3.4 59.8 1.0
HA3 C:GLY20 3.4 73.3 1.0
C C:GLY107 3.6 81.6 1.0
HA3 C:GLY108 3.7 90.8 1.0
HA3 C:GLY21 3.7 81.8 1.0
HA3 C:GLY106 3.8 90.8 1.0
CA C:GLY110 3.9 56.7 1.0
H C:THR109 3.9 82.5 1.0
CA C:GLY21 4.0 68.2 1.0
N C:THR109 4.0 68.7 1.0
CA C:GLY20 4.1 61.1 1.0
C C:GLY20 4.1 62.5 1.0
C C:GLY108 4.1 65.2 1.0
N C:GLY22 4.2 60.0 1.0
OG1 C:THR109 4.2 71.1 1.0
HA2 C:GLY20 4.2 73.3 1.0
CA C:GLY108 4.2 75.7 1.0
N C:GLY107 4.3 77.6 1.0
H C:GLY107 4.3 93.1 1.0
N C:GLY108 4.4 74.0 1.0
HA2 C:GLY110 4.4 68.1 1.0
C C:GLY106 4.5 76.3 1.0
C C:THR109 4.5 63.8 1.0
CA C:GLY107 4.6 84.5 1.0
CA C:GLY106 4.6 75.7 1.0
H C:THR111 4.6 71.6 1.0
C C:GLY21 4.6 57.6 1.0
O C:GLY108 4.7 63.5 1.0
HG1 C:THR109 4.7 85.3 1.0
CA C:THR109 4.8 71.9 1.0
HA2 C:GLY21 4.8 81.8 1.0
HA2 C:GLY107 5.0 0.3 1.0

Magnesium binding site 2 out of 2 in 6rvm

Go back to Magnesium Binding Sites List in 6rvm
Magnesium binding site 2 out of 2 in the Cell Division Protein Ftsz From Staphylococcus Aureus, Apo Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cell Division Protein Ftsz From Staphylococcus Aureus, Apo Form within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg406

b:72.9
occ:1.00
H D:GLY21 2.3 71.7 1.0
O D:GLY107 2.5 67.1 1.0
H D:GLY110 2.8 75.2 1.0
HA3 D:GLY108 3.0 80.3 1.0
N D:GLY21 3.1 59.7 1.0
CL D:CL405 3.3 76.5 1.0
HA3 D:GLY20 3.3 61.5 1.0
H D:THR109 3.4 75.4 1.0
C D:GLY107 3.6 75.9 1.0
CL D:CL403 3.6 85.4 1.0
N D:GLY110 3.6 62.7 1.0
HA3 D:GLY21 3.7 65.0 1.0
HA2 D:GLY20 3.7 61.5 1.0
N D:THR109 3.7 62.9 1.0
H D:GLY22 3.7 68.6 1.0
CA D:GLY108 3.8 67.0 1.0
CA D:GLY20 3.8 51.2 1.0
HA3 D:GLY110 3.9 69.4 1.0
C D:GLY20 4.0 58.0 1.0
CA D:GLY21 4.0 54.2 1.0
C D:GLY108 4.0 65.8 1.0
N D:GLY108 4.1 79.8 1.0
OG1 D:THR109 4.2 58.9 1.0
CA D:GLY110 4.3 57.8 1.0
N D:GLY22 4.5 57.2 1.0
HA2 D:GLY108 4.6 80.3 1.0
C D:THR109 4.6 58.0 1.0
CA D:THR109 4.7 64.4 1.0
HG1 D:THR109 4.7 70.7 1.0
H D:THR111 4.7 69.1 1.0
HA2 D:GLY21 4.7 65.0 1.0
C D:GLY21 4.8 62.5 1.0
CA D:GLY107 4.8 81.4 1.0
O D:GLY108 4.9 69.8 1.0
HA2 D:GLY110 4.9 69.4 1.0
HA2 D:GLY107 5.0 97.7 1.0
H D:GLY108 5.0 95.8 1.0

Reference:

S.Huecas, A.J.Canosa-Valls, L.Araujo-Bazan, F.M.Ruiz, D.V.Laurents, C.Fernandez-Tornero, J.M.Andreu. Nucleotide-Induced Folding of Cell Division Protein Ftsz From Staphylococcus Aureus. Febs J. 2020.
ISSN: ISSN 1742-464X
PubMed: 31997533
DOI: 10.1111/FEBS.15235
Page generated: Tue Dec 15 00:02:00 2020

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