Zinc in PDB 8srx: Crystal Structure of Bak-Bax Heterodimer with Lysopc

The structure of Crystal Structure of Bak-Bax Heterodimer with Lysopc, PDB code: 8srx was solved by J.M.Brouwer, P.E.Czabotar, P.M.Colman, M.S.Miller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.71 / 2.09
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	158.166, 45.562, 43.714, 90, 101.76, 90
R / Rfree (%)	21.6 / 26.5

The structure of Crystal Structure of Bak-Bax Heterodimer with Lysopc also contains other interesting chemical elements:

Chlorine	(Cl)	1 atom
Sodium	(Na)	2 atoms

The binding sites of Zinc atom in the Crystal Structure of Bak-Bax Heterodimer with Lysopc (pdb code 8srx). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Bak-Bax Heterodimer with Lysopc, PDB code: 8srx:

Zinc binding site 1 out of 1 in the Crystal Structure of Bak-Bax Heterodimer with Lysopc


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Bak-Bax Heterodimer with Lysopc within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn202 b:53.7 occ:1.00 O A:HOH305 2.2 38.1 1.0 ND1 A:HIS141 2.3 43.1 1.0 ND1 A:HIS145 2.3 41.8 1.0 CE1 A:HIS145 2.9 50.2 1.0 CE1 A:HIS141 3.1 40.3 1.0 O A:HOH321 3.2 45.4 1.0 CG A:HIS141 3.3 40.5 1.0 CG A:HIS145 3.4 41.6 1.0 CB A:HIS141 3.7 33.0 1.0 CA A:HIS141 3.7 32.1 1.0 NE2 A:HIS145 4.0 55.5 1.0 CB A:HIS145 4.0 42.2 1.0 NE2 A:HIS141 4.2 42.7 1.0 O A:HIS141 4.2 38.7 1.0 CD2 A:HIS145 4.2 49.8 1.0 NH2 A:ARG137 4.3 38.4 0.5 CD2 A:HIS141 4.3 33.6 1.0 C A:HIS141 4.5 37.1 1.0 NH1 A:ARG137 4.5 28.1 0.5 N A:HIS141 4.8 31.9 1.0 CZ A:ARG137 4.9 30.4 0.5

M.S.Miller, A.D.Cowan, J.M.Brouwer, S.T.Smyth, L.Peng, A.Z.Wardak, R.T.Uren, C.Luo, M.J.Roy, S.Shah, Z.Tan, G.E.Reid, P.M.Colman, P.E.Czabotar. Sequence Differences Between Bax and Bak Core Domains Manifest As Differences in Their Interactions with Lipids. Febs J. 2023.
ISSN: ISSN 1742-464X
PubMed: 38088212
DOI: 10.1111/FEBS.17031