Chlorine in PDB 3iql: Crystal Structure of the Rat Endophilin-A1 SH3 Domain

The structure of Crystal Structure of the Rat Endophilin-A1 SH3 Domain, PDB code: 3iql was solved by J.F.Trempe, G.Kozlov, E.M.Camacho, K.Gehring, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.40
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	64.338, 34.156, 62.729, 90.00, 107.79, 90.00
R / Rfree (%)	12.7 / 15.4

The binding sites of Chlorine atom in the Crystal Structure of the Rat Endophilin-A1 SH3 Domain (pdb code 3iql). 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 Rat Endophilin-A1 SH3 Domain, PDB code: 3iql:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of the Rat Endophilin-A1 SH3 Domain


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 Rat Endophilin-A1 SH3 Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1 b:16.1 occ:1.00 CE1 A:HIS352 3.4 16.5 1.0 O A:HOH24 3.5 13.2 1.0 NE2 A:HIS352 3.7 16.1 1.0 ND1 A:HIS352 4.6 15.4 1.0 O A:HOH110 4.7 20.0 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of the Rat Endophilin-A1 SH3 Domain


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 Rat Endophilin-A1 SH3 Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl2 b:15.3 occ:1.00 CE1 B:HIS352 3.4 16.8 1.0 O B:HOH11 3.5 10.9 1.0 NE2 B:HIS352 3.7 17.5 1.0 ND1 B:HIS352 4.6 15.9 1.0

J.F.Trempe, C.X.Chen, K.Grenier, E.M.Camacho, G.Kozlov, P.S.Mcpherson, K.Gehring, E.A.Fon. SH3 Domains From A Subset of Bar Proteins Define A Ubl-Binding Domain and Implicate Parkin in Synaptic Ubiquitination. Mol.Cell V. 36 1034 2009.
ISSN: ISSN 1097-2765
PubMed: 20064468
DOI: 10.1016/J.MOLCEL.2009.11.021