Chlorine in PDB 8trt: Structure of the EPHA2 Crd Bound to FABS1CE_C1, Monoclinic Form

All present enzymatic activity of Structure of the EPHA2 Crd Bound to FABS1CE_C1, Monoclinic Form:
2.7.10.1;

The structure of Structure of the EPHA2 Crd Bound to FABS1CE_C1, Monoclinic Form, PDB code: 8trt 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)	68.78 / 3.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	57.71, 182.135, 74.38, 90, 92.93, 90
R / Rfree (%)	19.4 / 24.4

The structure of Structure of the EPHA2 Crd Bound to FABS1CE_C1, Monoclinic Form also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Chlorine atom in the Structure of the EPHA2 Crd Bound to FABS1CE_C1, Monoclinic Form (pdb code 8trt). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Structure of the EPHA2 Crd Bound to FABS1CE_C1, Monoclinic Form, PDB code: 8trt:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Structure of the EPHA2 Crd Bound to FABS1CE_C1, Monoclinic Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the EPHA2 Crd Bound to FABS1CE_C1, Monoclinic Form within 5.0Å range: probe atom residue distance (Å) B Occ G:Cl301 b:62.0 occ:1.00 OG1 G:THR196 3.3 38.3 1.0 CA A:LEU202 3.9 37.0 1.0 OG A:SER201 4.0 37.6 1.0 O A:SER201 4.0 39.5 1.0 CG2 A:VAL193 4.1 39.7 1.0 N A:LEU202 4.2 36.7 1.0 C A:LEU202 4.2 36.6 1.0 C A:SER201 4.2 38.4 1.0 N A:SER203 4.3 37.7 1.0 OG G:SER194 4.4 38.4 1.0 CB G:THR196 4.5 38.3 1.0 OG A:SER203 4.6 37.5 1.0 CB A:SER201 4.8 39.2 1.0 O A:LEU202 4.8 35.9 1.0 CD1 A:LEU165 4.8 39.5 1.0 CB A:SER203 4.9 38.2 1.0

Chlorine binding site 2 out of 4 in the Structure of the EPHA2 Crd Bound to FABS1CE_C1, Monoclinic Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of the EPHA2 Crd Bound to FABS1CE_C1, Monoclinic Form within 5.0Å range: probe atom residue distance (Å) B Occ G:Cl302 b:52.1 occ:1.00 O G:THR218 3.3 50.4 1.0 OG G:SER220 3.8 48.0 1.0 C G:THR218 4.0 49.7 1.0 N G:THR219 4.7 49.2 1.0 CA G:THR218 4.8 51.7 1.0 N G:SER220 4.9 46.1 1.0 C G:THR219 4.9 47.2 1.0 CB G:SER220 4.9 46.3 1.0 CA G:THR219 4.9 48.3 1.0

Chlorine binding site 3 out of 4 in the Structure of the EPHA2 Crd Bound to FABS1CE_C1, Monoclinic Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure of the EPHA2 Crd Bound to FABS1CE_C1, Monoclinic Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl301 b:65.9 occ:1.00 CA B:SER156 3.3 66.8 1.0 O B:THR155 3.5 63.4 1.0 C B:SER156 3.6 69.3 1.0 N B:GLY157 4.1 65.8 1.0 O B:SER156 4.1 69.8 1.0 CB B:SER156 4.1 64.6 1.0 C B:THR155 4.2 63.9 1.0 N B:SER156 4.2 66.6 1.0 OG B:SER156 4.3 63.1 1.0 NZ C:LYS225 4.8 44.2 1.0

Chlorine binding site 4 out of 4 in the Structure of the EPHA2 Crd Bound to FABS1CE_C1, Monoclinic Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Structure of the EPHA2 Crd Bound to FABS1CE_C1, Monoclinic Form within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl301 b:56.1 occ:1.00 O C:THR218 3.3 52.6 1.0 OG C:SER220 3.5 49.8 1.0 C C:THR218 3.7 50.7 1.0 N C:THR219 4.1 50.2 1.0 C C:THR219 4.2 48.9 1.0 N C:SER220 4.2 46.0 1.0 CA C:THR219 4.3 49.0 1.0 CB C:SER220 4.4 49.1 1.0 CA C:THR218 4.5 53.5 1.0 O C:THR219 4.6 48.1 1.0 O C:GLY217 4.7 52.3 1.0 CA C:SER220 4.9 46.2 1.0 CG2 C:THR215 4.9 48.1 1.0

H.A.Bruce, A.U.Singer, E.V.Filippova, L.L.Blazer, J.J.Adams, L.Enderle, M.Ben-David, E.H.Radley, D.Y.L.Mao, V.Pau, S.Orlicky, F.Sicheri, I.Kourinov, S.Atwell, A.A.Kossiakoff, S.S.Sidhu. Engineered Antigen-Binding Fragments For Enhanced Crystallization of Antibody:Antigen Complexes. Protein Sci. E4824 2023.
ISSN: ESSN 1469-896X
PubMed: 37945533
DOI: 10.1002/PRO.4824