Chlorine in PDB 2vog: Structure of Mouse A1 Bound to the Bmf BH3-Domain

The structure of Structure of Mouse A1 Bound to the Bmf BH3-Domain, PDB code: 2vog was solved by C.Smits, P.E.Czabotar, M.G.Hinds, C.L.Day, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.81 / 1.9
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	66.654, 68.050, 32.136, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 23.1

The binding sites of Chlorine atom in the Structure of Mouse A1 Bound to the Bmf BH3-Domain (pdb code 2vog). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of Mouse A1 Bound to the Bmf BH3-Domain, PDB code: 2vog:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structure of Mouse A1 Bound to the Bmf BH3-Domain


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Mouse A1 Bound to the Bmf BH3-Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1150 b:27.0 occ:1.00 O A:HOH2026 2.9 37.2 1.0 ND1 B:HIS146 3.1 22.8 1.0 N A:TRP86 3.3 24.9 1.0 N A:GLY87 3.5 24.4 1.0 CB A:TRP86 3.7 25.0 1.0 CA B:HIS146 3.7 24.3 1.0 CB A:ASN85 3.8 24.2 1.0 CE1 B:PHE145 3.8 20.5 1.0 CE A:LYS147 3.9 35.2 1.0 CD1 B:PHE145 3.9 21.4 1.0 CA A:TRP86 3.9 25.2 1.0 CG B:HIS146 4.0 24.1 1.0 CB B:HIS146 4.0 23.7 1.0 OD1 A:ASN85 4.1 24.7 1.0 CE1 B:HIS146 4.1 24.8 1.0 CG A:ASN85 4.1 23.1 1.0 C A:TRP86 4.2 24.7 1.0 C A:ASN85 4.3 25.0 1.0 NZ A:LYS147 4.4 36.4 1.0 CD1 A:TRP86 4.5 25.6 1.0 N B:HIS146 4.5 22.7 1.0 CG A:TRP86 4.5 25.8 1.0 CA A:ASN85 4.5 24.1 1.0 CA A:GLY87 4.6 25.2 1.0 O B:HIS146 4.7 26.0 1.0 C B:HIS146 4.8 26.0 1.0 CD A:LYS147 5.0 34.1 1.0

Chlorine binding site 2 out of 2 in the Structure of Mouse A1 Bound to the Bmf BH3-Domain


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Mouse A1 Bound to the Bmf BH3-Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1151 b:26.2 occ:0.50 ND1 A:HIS10 3.0 31.3 1.0 O A:HOH2004 3.1 25.2 1.0 CG A:MET7 3.6 24.2 1.0 CB A:HIS10 3.7 24.7 1.0 CG A:HIS10 3.7 25.1 1.0 CA A:MET7 3.7 23.3 1.0 CB A:MET7 3.8 23.1 1.0 CE1 A:HIS10 4.0 28.9 1.0 O A:MET7 4.2 22.7 1.0 C A:MET7 4.5 23.3 1.0 SD A:MET7 4.5 23.7 1.0 N A:MET7 4.8 22.1 1.0 CD2 A:HIS10 4.9 28.4 1.0

C.Smits, P.E.Czabotar, M.G.Hinds, C.L.Day. Structural Plasticity Underpins Promiscuous Binding of the Prosurvival Protein A1. Structure V. 16 818 2008.
ISSN: ISSN 0969-2126
PubMed: 18462686
DOI: 10.1016/J.STR.2008.02.009