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Magnesium in PDB 6e0w: Crystal Structure of the Colanidase Tailspike Protein GP150 of Phage PHI92 Complexed with One Repeating Unit of Colanic Acid

Protein crystallography data

The structure of Crystal Structure of the Colanidase Tailspike Protein GP150 of Phage PHI92 Complexed with One Repeating Unit of Colanic Acid, PDB code: 6e0w was solved by M.Plattner, C.Browning, R.Gerardy-Schahn, M.M.Shneider, P.G.Leiman, D.Schwarzer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 61.46 / 1.80
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 117.623, 117.623, 308.282, 90.00, 90.00, 120.00
R / Rfree (%) 15.3 / 17.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Colanidase Tailspike Protein GP150 of Phage PHI92 Complexed with One Repeating Unit of Colanic Acid (pdb code 6e0w). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of the Colanidase Tailspike Protein GP150 of Phage PHI92 Complexed with One Repeating Unit of Colanic Acid, PDB code: 6e0w:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 6e0w

Go back to Magnesium Binding Sites List in 6e0w
Magnesium binding site 1 out of 3 in the Crystal Structure of the Colanidase Tailspike Protein GP150 of Phage PHI92 Complexed with One Repeating Unit of Colanic Acid


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 Colanidase Tailspike Protein GP150 of Phage PHI92 Complexed with One Repeating Unit of Colanic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg905

b:29.2
occ:1.00
O A:HOH1458 2.0 26.7 1.0
O A:HOH1071 2.0 30.8 1.0
O A:HOH1232 2.2 28.0 1.0
O A:HOH1021 2.2 28.6 1.0
OE2 A:GLU501 3.8 35.3 1.0
O A:HOH1180 4.0 36.7 1.0
O A:HOH1027 4.2 40.8 1.0
OD1 A:ASN467 4.4 30.9 1.0
O A:ASP499 4.4 26.3 1.0
O A:HOH1055 4.5 39.4 1.0
CA A:ASN467 4.9 29.6 1.0
CD A:GLU501 5.0 37.6 1.0

Magnesium binding site 2 out of 3 in 6e0w

Go back to Magnesium Binding Sites List in 6e0w
Magnesium binding site 2 out of 3 in the Crystal Structure of the Colanidase Tailspike Protein GP150 of Phage PHI92 Complexed with One Repeating Unit of Colanic Acid


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 Colanidase Tailspike Protein GP150 of Phage PHI92 Complexed with One Repeating Unit of Colanic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg907

b:27.5
occ:1.00
O B:HOH1154 2.1 28.5 1.0
O B:HOH1404 2.2 29.8 1.0
O B:ASP544 4.1 25.0 1.0
OE2 B:GLU547 4.2 33.7 1.0
OE1 B:GLU547 4.3 27.7 1.0
O B:HOH1123 4.4 28.6 1.0
O B:GLY507 4.5 25.6 1.0
N B:GLY507 4.5 24.8 1.0
CD B:GLU547 4.7 33.4 1.0
CD2 B:TYR508 4.7 31.3 1.0
CD B:PRO546 4.8 28.0 1.0

Magnesium binding site 3 out of 3 in 6e0w

Go back to Magnesium Binding Sites List in 6e0w
Magnesium binding site 3 out of 3 in the Crystal Structure of the Colanidase Tailspike Protein GP150 of Phage PHI92 Complexed with One Repeating Unit of Colanic Acid


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of the Colanidase Tailspike Protein GP150 of Phage PHI92 Complexed with One Repeating Unit of Colanic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg908

b:32.6
occ:1.00
O B:HOH1162 2.1 25.5 1.0
O B:HOH1152 2.1 33.4 1.0
O B:HOH1426 2.2 30.1 1.0
OD2 B:ASP383 4.1 26.6 1.0
OH B:TYR380 4.1 28.0 1.0
O B:HOH1102 4.2 37.8 1.0
ND1 B:HIS382 4.4 25.6 1.0
O B:HOH1574 4.5 72.6 1.0
CE1 B:HIS382 4.6 25.9 1.0
O B:HOH1427 4.8 41.3 1.0
O B:HOH1545 4.9 54.3 1.0

Reference:

C.Browning, M.Plattner, M.M.Shneider, R.Gerardy-Schahn, P.G.Leiman, D.Schwarzer. Crystal Structure of the Colanidase Tailspike Protein GP150 of Phage PHI92 Complexed with One Repeating Unit of Colanic Acid To Be Published.
Page generated: Mon Sep 30 23:46:15 2024

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