Bromine in PDB 1bk9: Phospholipase A2 Modified By Pbpb

All present enzymatic activity of Phospholipase A2 Modified By Pbpb:
3.1.1.4;

The structure of Phospholipase A2 Modified By Pbpb, PDB code: 1bk9 was solved by H.Zhao, L.Tang, X.Wang, Z.Lin, Y.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 2.00
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	82.820, 82.820, 32.800, 90.00, 90.00, 120.00
R / Rfree (%)	15.3 / 22.6

The structure of Phospholipase A2 Modified By Pbpb also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Bromine atom in the Phospholipase A2 Modified By Pbpb (pdb code 1bk9). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Phospholipase A2 Modified By Pbpb, PDB code: 1bk9:

Bromine binding site 1 out of 1 in the Phospholipase A2 Modified By Pbpb


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Phospholipase A2 Modified By Pbpb within 5.0Å range: probe atom residue distance (Å) B Occ A:Br400 b:27.4 occ:1.00 BR A:PBP400 0.0 27.4 1.0 CZ A:PBP400 1.9 23.0 1.0 CE2 A:PBP400 2.9 18.7 1.0 CE1 A:PBP400 2.9 20.1 1.0 C A:GLY30 3.8 16.4 1.0 CA A:GLY30 3.8 15.5 1.0 N A:TRP31 3.9 16.5 1.0 H A:TRP31 3.9 0.0 1.0 CD2 A:PBP400 4.2 17.8 1.0 CD1 A:PBP400 4.2 17.6 1.0 O A:GLY30 4.4 16.2 1.0 CA A:SER23 4.4 17.2 1.0 O A:SER23 4.5 16.1 1.0 CB A:SER23 4.6 18.5 1.0 CE3 A:TRP31 4.6 19.3 1.0 CA A:TRP31 4.6 16.6 1.0 N A:GLY30 4.6 12.0 1.0 CE A:MET19 4.7 52.1 1.0 CG A:PBP400 4.7 15.6 1.0 H A:GLY30 4.8 0.0 1.0 CB A:TRP31 4.9 18.1 1.0 C A:SER23 5.0 16.8 1.0

H.Zhao, L.Tang, X.Wang, Y.Zhou, Z.Lin. Structure of A Snake Venom Phospholipase A2 Modified By P-Bromo-Phenacyl-Bromide. Toxicon V. 36 875 1998.
ISSN: ISSN 0041-0101
PubMed: 9663694
DOI: 10.1016/S0041-0101(97)00169-4