Magnesium in PDB 1tye: Structural Basis For Allostery in Integrins and Binding of Ligand- Mimetic Therapeutics to the Platelet Receptor For Fibrinogen

The structure of Structural Basis For Allostery in Integrins and Binding of Ligand- Mimetic Therapeutics to the Platelet Receptor For Fibrinogen, PDB code: 1tye was solved by T.Xiao, J.Takagi, B.S.Coller, J.-H.Wang, T.A.Springer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.90
Space group	P 62
Cell size a, b, c (Å), α, β, γ (°)	332.093, 332.093, 88.288, 90.00, 90.00, 120.00
R / Rfree (%)	21.9 / 25.4

The structure of Structural Basis For Allostery in Integrins and Binding of Ligand- Mimetic Therapeutics to the Platelet Receptor For Fibrinogen also contains other interesting chemical elements:

Arsenic	(As)	3 atoms
Calcium	(Ca)	18 atoms

The binding sites of Magnesium atom in the Structural Basis For Allostery in Integrins and Binding of Ligand- Mimetic Therapeutics to the Platelet Receptor For Fibrinogen (pdb code 1tye). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Structural Basis For Allostery in Integrins and Binding of Ligand- Mimetic Therapeutics to the Platelet Receptor For Fibrinogen, PDB code: 1tye:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Structural Basis For Allostery in Integrins and Binding of Ligand- Mimetic Therapeutics to the Platelet Receptor For Fibrinogen


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structural Basis For Allostery in Integrins and Binding of Ligand- Mimetic Therapeutics to the Platelet Receptor For Fibrinogen within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1401 b:24.8 occ:1.00 O B:HOH1405 1.9 45.4 1.0 O2 B:CAC1301 1.9 0.4 1.0 OE1 B:GLU220 2.1 36.1 1.0 OG B:SER121 2.2 37.4 1.0 OG B:SER123 2.2 38.1 1.0 O B:HOH1404 2.2 28.2 1.0 CB B:SER121 3.2 39.6 1.0 CD B:GLU220 3.2 36.7 1.0 AS B:CAC1301 3.3 0.8 1.0 CB B:SER123 3.4 39.4 1.0 C1 B:CAC1301 3.6 0.8 1.0 CG B:GLU220 3.8 36.8 1.0 N B:SER123 4.0 40.6 1.0 OD1 B:ASP251 4.1 39.2 1.0 O B:ALA218 4.2 39.6 1.0 CA B:SER123 4.2 39.6 1.0 OE2 B:GLU220 4.3 37.0 1.0 OD1 B:ASP119 4.3 43.2 1.0 CA B:SER121 4.4 39.8 1.0 OD2 B:ASP119 4.4 41.0 1.0 O1 B:CAC1301 4.4 0.1 1.0 C B:SER121 4.5 40.1 1.0 C2 B:CAC1301 4.5 0.4 1.0 CB B:ALA252 4.5 44.4 1.0 N B:TYR122 4.7 40.3 1.0 N B:MET124 4.7 41.8 1.0 C B:SER123 4.8 39.4 1.0 CG B:ASP119 4.8 40.8 1.0 O B:SER121 4.9 40.9 1.0 CG B:ASP251 5.0 39.5 1.0

Magnesium binding site 2 out of 3 in the Structural Basis For Allostery in Integrins and Binding of Ligand- Mimetic Therapeutics to the Platelet Receptor For Fibrinogen


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structural Basis For Allostery in Integrins and Binding of Ligand- Mimetic Therapeutics to the Platelet Receptor For Fibrinogen within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg1408 b:18.8 occ:1.00 O2 D:CAC1302 1.9 96.9 1.0 O D:HOH1412 2.0 39.2 1.0 OG D:SER123 2.0 38.5 1.0 OE1 D:GLU220 2.0 27.2 1.0 O D:HOH1411 2.0 26.4 1.0 OG D:SER121 2.2 30.8 1.0 CD D:GLU220 3.0 27.0 1.0 CB D:SER123 3.2 40.8 1.0 CB D:SER121 3.3 37.0 1.0 AS D:CAC1302 3.5 97.1 1.0 CG D:GLU220 3.5 28.3 1.0 OD1 D:ASP251 3.8 46.6 1.0 C1 D:CAC1302 3.9 96.8 1.0 O D:ALA218 4.0 33.8 1.0 N D:SER123 4.0 40.2 1.0 OE2 D:GLU220 4.0 22.9 1.0 CA D:SER123 4.2 42.2 1.0 OD2 D:ASP119 4.3 38.5 1.0 OD1 D:ASP119 4.3 42.4 1.0 C2 D:CAC1302 4.5 98.0 1.0 CB D:ALA252 4.5 43.4 1.0 CA D:SER121 4.5 38.9 1.0 C D:SER121 4.6 40.6 1.0 O1 D:CAC1302 4.6 98.1 1.0 CG D:ASP119 4.7 42.5 1.0 CG D:ASP251 4.9 45.2 1.0 O D:SER121 4.9 43.5 1.0 C D:SER123 4.9 44.4 1.0 N D:TYR122 4.9 40.8 1.0

Magnesium binding site 3 out of 3 in the Structural Basis For Allostery in Integrins and Binding of Ligand- Mimetic Therapeutics to the Platelet Receptor For Fibrinogen


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structural Basis For Allostery in Integrins and Binding of Ligand- Mimetic Therapeutics to the Platelet Receptor For Fibrinogen within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg1415 b:32.2 occ:1.00 O F:HOH1419 2.0 40.2 1.0 OE1 F:GLU220 2.0 46.1 1.0 O2 F:CAC1303 2.0 0.9 1.0 OG F:SER121 2.1 50.9 1.0 OG F:SER123 2.1 54.1 1.0 O F:HOH1418 2.1 22.0 1.0 CB F:SER121 3.0 55.7 1.0 CD F:GLU220 3.1 46.2 1.0 CB F:SER123 3.3 58.8 1.0 AS F:CAC1303 3.4 0.9 1.0 C1 F:CAC1303 3.6 1.0 1.0 CG F:GLU220 3.7 47.0 1.0 N F:SER123 3.9 59.4 1.0 OD1 F:ASP119 4.0 60.8 1.0 OE2 F:GLU220 4.1 46.3 1.0 CA F:SER123 4.2 60.2 1.0 OD2 F:ASP119 4.2 60.1 1.0 CA F:SER121 4.2 58.1 1.0 OD1 F:ASP251 4.2 63.9 1.0 C2 F:CAC1303 4.3 1.0 1.0 O F:ALA218 4.3 48.5 1.0 C F:SER121 4.3 59.0 1.0 CG F:ASP119 4.5 61.1 1.0 O1 F:CAC1303 4.6 0.6 1.0 O F:SER121 4.7 60.3 1.0 N F:TYR122 4.7 59.5 1.0 C F:SER123 4.7 62.0 1.0 N F:MET124 4.8 64.8 1.0 N F:SER121 4.9 59.0 1.0 CG F:MET124 4.9 68.0 1.0

T.Xiao, J.Takagi, B.S.Coller, J.-H.Wang, T.A.Springer. Structural Basis For Allostery in Integrins and Binding to Fibrinogen-Mimetic Therapeutics Nature V. 432 59 2004.
ISSN: ISSN 0028-0836
PubMed: 15378069
DOI: 10.1038/NATURE02976