Arsenic 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:

Magnesium	(Mg)	3 atoms
Calcium	(Ca)	18 atoms

The binding sites of Arsenic 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 Arsenic atom.
In total 3 binding sites of Arsenic 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 Arsenic binding site number: 1; 2; 3;

Arsenic 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 Arsenic with other atoms in the As 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:As1301 b:0.8 occ:1.00 AS B:CAC1301 0.0 0.8 1.0 O1 B:CAC1301 1.7 0.1 1.0 O2 B:CAC1301 1.8 0.4 1.0 C2 B:CAC1301 1.9 0.4 1.0 C1 B:CAC1301 2.0 0.8 1.0 MG B:MG1401 3.3 24.8 1.0 OE1 B:GLU220 3.5 36.1 1.0 N B:TYR122 3.6 40.3 1.0 N B:SER123 3.7 40.6 1.0 CB B:SER121 3.8 39.6 1.0 O B:ASN215 3.9 34.0 1.0 O B:HOH1404 3.9 28.2 1.0 CB B:TYR122 4.0 41.9 1.0 OG B:SER121 4.0 37.4 1.0 OG B:SER123 4.0 38.1 1.0 CB B:ASN215 4.1 35.9 1.0 CA B:TYR122 4.1 40.3 1.0 N B:ASN215 4.2 36.1 1.0 CB B:SER123 4.3 39.4 1.0 C B:TYR122 4.4 40.5 1.0 C B:SER121 4.4 40.1 1.0 C B:ASN215 4.5 33.5 1.0 CA B:ASN215 4.6 33.9 1.0 CD B:GLU220 4.6 36.7 1.0 CA B:SER123 4.6 39.6 1.0 CA B:SER121 4.6 39.8 1.0 OD1 B:ASN215 4.8 42.0 1.0 OE2 B:GLU220 4.9 37.0 1.0 O B:ASP217 4.9 31.5 1.0 CG B:ASN215 4.9 39.1 1.0

Arsenic 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 Arsenic with other atoms in the As 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:As1302 b:97.1 occ:1.00 AS D:CAC1302 0.0 97.1 1.0 O1 D:CAC1302 1.7 98.1 1.0 O2 D:CAC1302 1.8 96.9 1.0 C2 D:CAC1302 1.9 98.0 1.0 C1 D:CAC1302 2.0 96.8 1.0 MG D:MG1408 3.5 18.8 1.0 OE1 D:GLU220 3.6 27.2 1.0 N D:SER123 3.7 40.2 1.0 N D:TYR122 3.7 40.8 1.0 CB D:SER121 3.8 37.0 1.0 CB D:ASN215 3.9 34.2 1.0 OG D:SER121 3.9 30.8 1.0 CB D:TYR122 4.0 42.0 1.0 O D:ASN215 4.0 31.5 1.0 O D:HOH1411 4.1 26.4 1.0 OG D:SER123 4.1 38.5 1.0 CA D:TYR122 4.2 40.2 1.0 N D:ASN215 4.2 34.6 1.0 CB D:SER123 4.3 40.8 1.0 C D:TYR122 4.4 40.0 1.0 C D:SER121 4.4 40.6 1.0 C D:ASN215 4.5 32.8 1.0 CD D:GLU220 4.5 27.0 1.0 CA D:ASN215 4.6 33.0 1.0 CA D:SER123 4.6 42.2 1.0 CA D:SER121 4.6 38.9 1.0 OE2 D:GLU220 4.7 22.9 1.0 CG D:ASN215 5.0 37.0 1.0

Arsenic 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 Arsenic with other atoms in the As 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:As1303 b:0.9 occ:1.00 AS F:CAC1303 0.0 0.9 1.0 O1 F:CAC1303 1.7 0.6 1.0 O2 F:CAC1303 1.8 0.9 1.0 C2 F:CAC1303 1.9 1.0 1.0 C1 F:CAC1303 2.0 1.0 1.0 MG F:MG1415 3.4 32.2 1.0 OE1 F:GLU220 3.7 46.1 1.0 N F:SER123 3.7 59.4 1.0 O F:HOH1418 3.7 22.0 1.0 N F:TYR122 3.8 59.5 1.0 CB F:SER121 3.9 55.7 1.0 OG F:SER123 4.0 54.1 1.0 O F:ASN215 4.0 43.2 1.0 CB F:ASN215 4.1 47.6 1.0 OG F:SER121 4.1 50.9 1.0 CB F:SER123 4.2 58.8 1.0 CB F:TYR122 4.2 60.6 1.0 CA F:TYR122 4.3 59.9 1.0 N F:ASN215 4.3 48.8 1.0 C F:TYR122 4.4 59.9 1.0 C F:SER121 4.5 59.0 1.0 CA F:SER123 4.5 60.2 1.0 C F:ASN215 4.5 44.5 1.0 CA F:ASN215 4.6 46.0 1.0 CA F:SER121 4.7 58.1 1.0 CD F:GLU220 4.7 46.2 1.0 O F:ASP217 4.9 39.8 1.0 OE2 F:GLU220 5.0 46.3 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