Magnesium in PDB 9lgu: Crystal Structure of Bcl-Xl in Complex with Stapled Hrk Peptide

The structure of Crystal Structure of Bcl-Xl in Complex with Stapled Hrk Peptide, PDB code: 9lgu was solved by H.Wei, M.Guo, J.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.05 / 2.97
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	71.59, 111.91, 84.14, 90, 109.52, 90
R / Rfree (%)	25.7 / 30.3

The binding sites of Magnesium atom in the Crystal Structure of Bcl-Xl in Complex with Stapled Hrk Peptide (pdb code 9lgu). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Crystal Structure of Bcl-Xl in Complex with Stapled Hrk Peptide, PDB code: 9lgu:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in the Crystal Structure of Bcl-Xl in Complex with Stapled Hrk Peptide


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Bcl-Xl in Complex with Stapled Hrk Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:26.8 occ:1.00 OG A:SER110 2.2 40.8 1.0 CB A:SER110 3.6 52.6 1.0 OD2 A:ASP107 4.3 35.7 1.0 OE1 A:GLU153 4.4 24.9 1.0 CA A:SER110 4.5 45.0 1.0 OD2 A:ASP156 4.5 41.0 1.0 OE2 A:GLU153 4.5 44.9 1.0 CD A:GLU153 4.9 29.4 1.0

Magnesium binding site 2 out of 5 in the Crystal Structure of Bcl-Xl in Complex with Stapled Hrk Peptide


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Bcl-Xl in Complex with Stapled Hrk Peptide within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg301 b:46.6 occ:1.00 OG C:SER110 2.4 41.9 1.0 CB C:SER110 3.8 55.3 1.0 OE1 C:GLU153 4.3 41.0 1.0 OD2 C:ASP107 4.3 42.0 1.0 OD2 C:ASP156 4.6 40.3 1.0 CA C:SER110 4.6 52.9 1.0 OE2 C:GLU153 4.8 56.0 1.0 CD C:GLU153 4.9 42.4 1.0

Magnesium binding site 3 out of 5 in the Crystal Structure of Bcl-Xl in Complex with Stapled Hrk Peptide


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Bcl-Xl in Complex with Stapled Hrk Peptide within 5.0Å range: probe atom residue distance (Å) B Occ I:Mg301 b:22.0 occ:1.00 OG I:SER110 2.1 64.4 1.0 OE1 I:GLU153 3.2 39.4 1.0 CB I:SER110 3.5 55.0 1.0 CD I:GLU153 4.1 41.2 1.0 OD2 I:ASP107 4.1 39.0 1.0 CA I:SER110 4.2 50.5 1.0 OE2 I:GLU153 4.3 59.6 1.0 N I:SER110 4.8 44.6 1.0 OD2 I:ASP156 4.8 53.4 1.0

Magnesium binding site 4 out of 5 in the Crystal Structure of Bcl-Xl in Complex with Stapled Hrk Peptide


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Bcl-Xl in Complex with Stapled Hrk Peptide within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg101 b:28.1 occ:1.00 CE B:MK835 4.0 42.6 1.0 CG B:MK835 4.1 42.7 1.0 CE B:MK839 4.3 41.7 1.0 CB1 B:MK835 4.5 42.1 1.0 CG B:MK839 4.7 43.4 1.0 CD B:MK835 4.7 42.6 1.0 OE2 E:GLU184 4.8 47.2 1.0 NZ B:LYS38 4.8 43.8 1.0 CD B:LYS38 4.8 42.1 1.0 O B:MK835 5.0 44.8 1.0 CB1 D:MK839 5.0 30.9 1.0

Magnesium binding site 5 out of 5 in the Crystal Structure of Bcl-Xl in Complex with Stapled Hrk Peptide


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Crystal Structure of Bcl-Xl in Complex with Stapled Hrk Peptide within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg101 b:22.8 occ:1.00 CE D:MK835 4.0 19.8 1.0 CG D:MK835 4.2 13.2 1.0 CE D:MK839 4.3 18.8 1.0 CB1 D:MK835 4.6 22.7 1.0 CG D:MK839 4.7 22.9 1.0 CD D:LYS38 4.7 20.8 1.0 CD D:MK835 4.8 16.6 1.0 CB1 B:MK839 4.9 40.4 1.0 O D:MK835 5.0 24.2 1.0 OE2 G:GLU184 5.0 50.7 1.0 NZ D:LYS38 5.0 31.0 1.0

H.Wei, J.Wang, M.Guo, S.Dai. Molecular Mechanisms Underlying Hrk Interaction with Bcl-Xl and Bcl-2 Reveal Specificity Determinants For Selective BH3 Mimetics To Be Published.