Zinc in PDB 3io8: BIML12F in Complex with Bcl-Xl

The structure of BIML12F in Complex with Bcl-Xl, PDB code: 3io8 was solved by P.M.Colman, E.F.Lee, W.D.Fairlie, B.J.Smith, P.E.Czabotar, H.Yang, B.E.Sleebs, G.Lessene, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.30 / 2.30
Space group	P 62
Cell size a, b, c (Å), α, β, γ (°)	65.717, 65.717, 170.094, 90.00, 90.00, 120.00
R / Rfree (%)	18.5 / 23.1

The binding sites of Zinc atom in the BIML12F in Complex with Bcl-Xl (pdb code 3io8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the BIML12F in Complex with Bcl-Xl, PDB code: 3io8:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the BIML12F in Complex with Bcl-Xl


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of BIML12F in Complex with Bcl-Xl within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn210 b:52.9 occ:1.00 O A:HOH211 2.7 35.5 1.0 O A:HOH217 3.2 49.9 1.0 N A:PRO-3 3.8 37.9 1.0 CA A:PRO-3 4.7 36.5 1.0 CD A:PRO-3 4.8 36.4 1.0 O A:PRO-3 4.9 38.2 1.0 C A:PRO-3 4.9 39.5 1.0 CD2 A:LEU-2 4.9 41.4 1.0

Zinc binding site 2 out of 3 in the BIML12F in Complex with Bcl-Xl


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of BIML12F in Complex with Bcl-Xl within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn210 b:58.3 occ:1.00 ND1 C:HIS113 2.3 56.7 1.0 O C:HOH215 2.6 44.4 1.0 CE1 C:HIS113 3.3 59.2 1.0 CG C:HIS113 3.3 61.8 1.0 CB C:HIS113 3.6 61.5 1.0 CA C:HIS113 4.3 63.6 1.0 NE2 C:HIS113 4.4 63.8 1.0 CD2 C:HIS113 4.5 63.7 1.0

Zinc binding site 3 out of 3 in the BIML12F in Complex with Bcl-Xl


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of BIML12F in Complex with Bcl-Xl within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn211 b:84.8 occ:1.00 N C:GLY-4 2.6 56.3 1.0 CA C:GLY-4 2.7 50.3 1.0 O C:GLY-4 3.3 48.1 1.0 C C:GLY-4 3.4 47.2 1.0 N C:PRO-3 4.6 47.7 1.0

E.F.Lee, P.E.Czabotar, H.Yang, B.E.Sleebs, G.Lessene, P.M.Colman, B.J.Smith, W.D.Fairlie. Conformational Changes in Bcl-2 Pro-Survival Proteins Determine Their Capacity to Bind Ligands. J.Biol.Chem. V. 284 30508 2009.
ISSN: ISSN 0021-9258
PubMed: 19726685
DOI: 10.1074/JBC.M109.040725