Sodium in PDB 8trv: Structure of the EPHA2 Lbdcrd Bound to FABS1C_C1

All present enzymatic activity of Structure of the EPHA2 Lbdcrd Bound to FABS1C_C1:
2.7.10.1;

The structure of Structure of the EPHA2 Lbdcrd Bound to FABS1C_C1, PDB code: 8trv was solved by A.U.Singer, H.A.Bruce, L.Blazer, J.J.Adams, F.Sicheri, S.S.Sidhu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	131.72 / 3.25
Space group	P 21 2 21
Cell size a, b, c (Å), α, β, γ (°)	73.933, 110.558, 263.443, 90, 90, 90
R / Rfree (%)	21.7 / 27.2

The structure of Structure of the EPHA2 Lbdcrd Bound to FABS1C_C1 also contains other interesting chemical elements:

Iodine	(I)	5 atoms
Chlorine	(Cl)	10 atoms

The binding sites of Sodium atom in the Structure of the EPHA2 Lbdcrd Bound to FABS1C_C1 (pdb code 8trv). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 4 binding sites of Sodium where determined in the Structure of the EPHA2 Lbdcrd Bound to FABS1C_C1, PDB code: 8trv:
Jump to Sodium binding site number: 1; 2; 3; 4;

Sodium binding site 1 out of 4 in the Structure of the EPHA2 Lbdcrd Bound to FABS1C_C1


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of the EPHA2 Lbdcrd Bound to FABS1C_C1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Na403 b:156.4 occ:1.00 OE2 A:GLU166 3.8 141.6 1.0 OE1 A:GLU166 3.9 142.5 1.0 CD A:GLU166 4.2 141.7 1.0 OD2 A:ASP148 4.3 166.2 1.0 CB A:ASP148 4.4 168.2 1.0 O A:PRO147 4.6 161.0 1.0 CG A:ASP148 4.7 167.0 1.0 O A:ALA146 4.7 154.9 1.0

Sodium binding site 2 out of 4 in the Structure of the EPHA2 Lbdcrd Bound to FABS1C_C1


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Structure of the EPHA2 Lbdcrd Bound to FABS1C_C1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Na404 b:145.0 occ:1.00 OD1 A:ASP143 2.3 152.3 1.0 OD2 A:ASP143 2.3 152.1 1.0 CG A:ASP143 2.6 151.9 1.0 CB A:ASP143 4.1 151.0 1.0 O A:THR144 4.2 157.7 1.0 N A:THR144 4.2 156.6 1.0 CA A:ASP143 4.7 151.2 1.0 C A:ASP143 4.7 152.0 1.0 C A:THR144 4.8 157.6 1.0 CB A:THR144 4.8 156.8 1.0 CA A:THR144 4.9 157.1 1.0

Sodium binding site 3 out of 4 in the Structure of the EPHA2 Lbdcrd Bound to FABS1C_C1


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 3 of Structure of the EPHA2 Lbdcrd Bound to FABS1C_C1 within 5.0Å range: probe atom residue distance (Å) B Occ C:Na303 b:81.9 occ:1.00 OG C:SER201 2.9 90.5 1.0 OE1 C:GLN195 3.3 99.3 1.0 OG G:SER149 3.3 97.1 1.0 NE2 G:GLN178 3.3 92.7 1.0 CG C:LYS167 3.4 97.2 1.0 CE C:LYS167 3.5 104.4 1.0 CB C:SER201 3.7 91.5 1.0 NZ C:LYS167 3.7 106.1 1.0 OG1 G:THR198 3.8 92.2 1.0 CD C:LYS167 3.8 99.7 1.0 CG2 G:THR196 4.0 86.8 1.0 CD C:GLN195 4.2 97.3 1.0 CB G:SER149 4.2 97.7 1.0 CD1 C:LEU165 4.5 82.0 1.0 CD2 C:LEU165 4.6 84.4 1.0 CD G:GLN178 4.6 96.8 1.0 CB C:LYS167 4.7 94.7 1.0 NE2 C:GLN195 4.7 94.5 1.0

Sodium binding site 4 out of 4 in the Structure of the EPHA2 Lbdcrd Bound to FABS1C_C1


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 4 of Structure of the EPHA2 Lbdcrd Bound to FABS1C_C1 within 5.0Å range: probe atom residue distance (Å) B Occ D:Na303 b:86.7 occ:1.00 OD1 D:ASN223 3.0 102.2 1.0 O D:THR229 3.3 99.1 1.0 N D:THR229 3.8 102.0 1.0 C D:THR229 3.9 100.5 1.0 C D:ASN228 3.9 100.6 1.0 CG D:ASN223 3.9 98.3 1.0 CA D:ASN228 4.1 103.7 1.0 CA D:LYS225 4.2 101.0 1.0 O D:HIS224 4.3 99.9 1.0 N D:LYS225 4.3 98.2 1.0 ND2 D:ASN223 4.4 96.2 1.0 C D:HIS224 4.4 98.2 1.0 O D:ASN228 4.4 103.5 1.0 CA D:THR229 4.5 101.0 1.0 CB D:LYS230 4.5 100.4 1.0 N D:LYS230 4.5 96.6 1.0 N D:HIS224 4.7 95.6 1.0 CB D:LYS225 4.8 101.2 1.0 CA D:LYS230 4.9 96.6 1.0 N D:ASN228 5.0 101.5 1.0

J.J.Adams, H.A.Bruce, L.Ploder, J.Garcia, G.Khutoreskaya, N.Jarvik, L.E.Costa, M.Gorelik, I.Pot, F.Sicheri, L.L.Blazer, A.U.Singer, S.S.Sidhu. Synthetic Antibodies Targeting EPHA2 Induce Diverse Signaling-Competent Clusters with Differential Activation To Be Published.