Chlorine in PDB 3s8n: Crystal Structure of the GRB2 SH2 Domain in Complex with A Pyxn- Derived Tripeptide

The structure of Crystal Structure of the GRB2 SH2 Domain in Complex with A Pyxn- Derived Tripeptide, PDB code: 3s8n was solved by J.H.Clements, F.M.Stephen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.25 / 1.71
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	42.071, 42.071, 109.006, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 24.4

The binding sites of Chlorine atom in the Crystal Structure of the GRB2 SH2 Domain in Complex with A Pyxn- Derived Tripeptide (pdb code 3s8n). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of the GRB2 SH2 Domain in Complex with A Pyxn- Derived Tripeptide, PDB code: 3s8n:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of the GRB2 SH2 Domain in Complex with A Pyxn- Derived Tripeptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the GRB2 SH2 Domain in Complex with A Pyxn- Derived Tripeptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl4 b:37.5 occ:1.00 N A:SER139 3.3 24.9 1.0 NE2 A:GLN145 3.5 27.9 1.0 CA A:THR138 3.9 24.8 1.0 CE2 A:PHE147 4.0 27.1 1.0 CB A:SER139 4.1 22.7 1.0 C A:THR138 4.1 25.8 1.0 OE1 A:GLN145 4.1 28.1 1.0 CG2 A:THR138 4.1 25.7 1.0 CZ A:PHE147 4.2 27.4 1.0 CD A:GLN145 4.2 25.1 1.0 CA A:SER139 4.3 23.6 1.0 CB A:THR138 4.5 25.9 1.0 O A:SER137 4.6 27.7 1.0 OG1 A:THR138 4.8 26.8 1.0 N A:THR138 5.0 26.2 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of the GRB2 SH2 Domain in Complex with A Pyxn- Derived Tripeptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the GRB2 SH2 Domain in Complex with A Pyxn- Derived Tripeptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl5 b:54.5 occ:1.00 O A:HOH15 3.3 32.0 1.0 NH1 A:ARG136 3.3 27.4 1.0 CD A:ARG136 3.5 23.6 1.0 CG A:ARG136 4.0 20.7 1.0 CB A:ARG136 4.0 22.8 1.0 O A:LEU148 4.0 24.1 1.0 CZ A:ARG136 4.2 26.3 1.0 NE A:ARG136 4.3 23.4 1.0 CA A:ARG149 4.8 24.8 1.0

J.M.Myslinski, J.E.Delorbe, J.H.Clements, S.F.Martin. Protein-Ligand Interactions: Thermodynamic Effects Associated with Increasing Nonpolar Surface Area. J.Am.Chem.Soc. V. 133 18518 2011.
ISSN: ISSN 0002-7863
PubMed: 22007755
DOI: 10.1021/JA2068752