Sodium in PDB 9igl: Crystal Structure of P. Syringae Phosphinothricin Acetyltransferase PSPTO_3321 in Complex with L-Phosphinothricin

The structure of Crystal Structure of P. Syringae Phosphinothricin Acetyltransferase PSPTO_3321 in Complex with L-Phosphinothricin, PDB code: 9igl was solved by A.M.Davies, D.Trentham, B.J.Sutton, P.R.Brown, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	77.88 / 2.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	138.577, 97.596, 117.588, 90, 111.19, 90
R / Rfree (%)	20.5 / 24.9

The binding sites of Sodium atom in the Crystal Structure of P. Syringae Phosphinothricin Acetyltransferase PSPTO_3321 in Complex with L-Phosphinothricin (pdb code 9igl). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of P. Syringae Phosphinothricin Acetyltransferase PSPTO_3321 in Complex with L-Phosphinothricin, PDB code: 9igl:

Sodium binding site 1 out of 1 in the Crystal Structure of P. Syringae Phosphinothricin Acetyltransferase PSPTO_3321 in Complex with L-Phosphinothricin


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of P. Syringae Phosphinothricin Acetyltransferase PSPTO_3321 in Complex with L-Phosphinothricin within 5.0Å range: probe atom residue distance (Å) B Occ C:Na204 b:30.8 occ:1.00 OH C:TYR75 2.7 33.6 1.0 OH D:TYR75 3.3 40.5 1.0 NH2 D:ARG76 3.6 38.2 1.0 NH2 C:ARG76 3.6 34.7 1.0 CZ C:TYR75 3.7 33.3 1.0 CE1 C:TYR75 3.8 31.1 1.0 CE1 D:TYR75 4.1 38.0 1.0 CZ D:TYR75 4.1 37.1 1.0 NE D:ARG76 4.1 38.5 1.0 NE C:ARG76 4.2 32.4 1.0 CZ C:ARG76 4.3 38.4 1.0 CZ D:ARG76 4.3 38.1 1.0 CE2 D:PHE147 4.7 27.5 1.0 CE2 C:PHE147 4.8 24.8 1.0 CE2 C:TYR75 4.9 26.6 1.0

A.M.Davies, D.Trentham, B.J.Sutton, P.R.Brown. Structure and Activity of A Phosphinothricin N-Acetyltransferase (PSPTO_3321) From Pseudomonas Syringae Pv. Tomato DC3000 Biochem.Biophys.Res.Commun. 2025.
ISSN: ESSN 1090-2104
DOI: 10.1016/J.BBRC.2025.151539