Chlorine in PDB 4yj4: Crystal Structure of Bcl-Xl in Complex with the Bim BH3 Domain Containing ILE155-to-Arg and GLU158-to-Phosphoserine Mutations

The structure of Crystal Structure of Bcl-Xl in Complex with the Bim BH3 Domain Containing ILE155-to-Arg and GLU158-to-Phosphoserine Mutations, PDB code: 4yj4 was solved by B.Ku, N.-C.Ha, B.-H.Oh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.10
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	72.926, 72.926, 75.458, 90.00, 90.00, 120.00
R / Rfree (%)	18.3 / 21.1

The binding sites of Chlorine atom in the Crystal Structure of Bcl-Xl in Complex with the Bim BH3 Domain Containing ILE155-to-Arg and GLU158-to-Phosphoserine Mutations (pdb code 4yj4). 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 Bcl-Xl in Complex with the Bim BH3 Domain Containing ILE155-to-Arg and GLU158-to-Phosphoserine Mutations, PDB code: 4yj4:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Bcl-Xl in Complex with the Bim BH3 Domain Containing ILE155-to-Arg and GLU158-to-Phosphoserine Mutations


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 Bcl-Xl in Complex with the Bim BH3 Domain Containing ILE155-to-Arg and GLU158-to-Phosphoserine Mutations within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl201 b:22.8 occ:1.00 O B:HOH305 3.2 14.4 1.0 NH2 B:ARG155 3.2 13.0 1.0 NH1 B:ARG155 3.4 13.5 1.0 OE2 B:GLU151 3.5 18.0 1.0 CD B:GLU151 3.7 15.5 1.0 CZ B:ARG155 3.7 9.8 1.0 OE1 B:GLU151 3.9 14.8 1.0 CB A:ALA104 4.2 21.6 1.0 CG B:GLU151 4.3 14.5 1.0 O A:HOH304 4.5 24.8 1.0 O A:ALA104 4.5 22.1 1.0 CA A:ALA104 5.0 21.8 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Bcl-Xl in Complex with the Bim BH3 Domain Containing ILE155-to-Arg and GLU158-to-Phosphoserine Mutations


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 Bcl-Xl in Complex with the Bim BH3 Domain Containing ILE155-to-Arg and GLU158-to-Phosphoserine Mutations within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl202 b:14.6 occ:1.00 NH2 A:ARG132 2.8 35.2 1.0 NH1 B:ARG153 3.3 9.8 1.0 NE2 B:GLN150 3.5 14.9 1.0 CZ B:ARG153 3.8 10.1 1.0 NE B:ARG153 3.9 11.8 1.0 CZ A:ARG132 4.0 34.4 1.0 OE1 B:GLN150 4.0 12.7 1.0 CD B:GLN150 4.1 12.9 1.0 CD A:ARG132 4.6 31.4 1.0 NE A:ARG132 4.7 33.8 1.0 NH2 B:ARG153 4.8 12.0 1.0 OD2 A:ASP133 4.8 15.3 1.0 NH1 A:ARG132 4.9 36.9 1.0 OE1 A:GLU129 4.9 16.7 1.0

J.S.Kim, B.Ku, T.G.Woo, A.Y.Oh, Y.S.Jung, Y.M.Soh, J.H.Yeom, K.Lee, B.J.Park, B.H.Oh, N.C.Ha. Conversion of Cell-Survival Activity of Akt Into Apoptotic Death of Cancer Cells By Two Mutations on the Bim BH3 Domain. Cell Death Dis V. 6 E1804 2015.
ISSN: ISSN 2041-4889
PubMed: 26136077
DOI: 10.1038/CDDIS.2015.118