Chlorine in PDB 8ghh: Crystal Structure of Staphylococcus Aureus Lysophosphatidylglycerol Phospholipase D

All present enzymatic activity of Crystal Structure of Staphylococcus Aureus Lysophosphatidylglycerol Phospholipase D:
3.1.4.46;

The structure of Crystal Structure of Staphylococcus Aureus Lysophosphatidylglycerol Phospholipase D, PDB code: 8ghh was solved by C.O.Rock, M.Yun, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.56 / 2.10
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	107.956, 107.956, 138.381, 90, 90, 90
R / Rfree (%)	18.8 / 21.5

The binding sites of Chlorine atom in the Crystal Structure of Staphylococcus Aureus Lysophosphatidylglycerol Phospholipase D (pdb code 8ghh). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Staphylococcus Aureus Lysophosphatidylglycerol Phospholipase D, PDB code: 8ghh:

Chlorine binding site 1 out of 1 in the Crystal Structure of Staphylococcus Aureus Lysophosphatidylglycerol Phospholipase D


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 Staphylococcus Aureus Lysophosphatidylglycerol Phospholipase D within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl410 b:97.2 occ:1.00 O A:HOH522 3.1 74.5 1.0 CA A:GLY103 3.7 55.2 1.0 N A:SER104 3.7 54.1 1.0 NE2 A:HIS110 3.7 84.3 1.0 O A:SER104 3.9 59.3 1.0 C A:GLY103 4.2 54.1 1.0 CD2 A:LEU118 4.3 49.5 1.0 CD2 A:HIS110 4.4 82.7 1.0 O A:HOH552 4.5 58.6 1.0 CE1 A:HIS110 4.7 87.7 1.0 OG A:SER104 4.8 68.5 1.0 CA A:SER104 4.8 59.9 1.0 C A:SER104 4.8 60.9 1.0 N A:GLY103 4.9 53.1 1.0

C.Subramanian, M.K.Yun, M.M.Frank, C.O.Rock. Lysophosphatidylglycerol (Lpg) Phospholipase D Maintains Membrane Homeostasis in Staphylococcus Aureus By Converting Lpg to Lysophosphatidic Acid. J.Biol.Chem. V. 299 04863 2023.
ISSN: ESSN 1083-351X
PubMed: 37236358
DOI: 10.1016/J.JBC.2023.104863