Sodium in PDB 6mlg: Crystal Structure of the Periplasmic Lysine-, Arginine-, Ornithine- Binding Protein (Lao) R77A Mutant From Salmonella Typhimurium Complexed with Arginine

The structure of Crystal Structure of the Periplasmic Lysine-, Arginine-, Ornithine- Binding Protein (Lao) R77A Mutant From Salmonella Typhimurium Complexed with Arginine, PDB code: 6mlg was solved by S.Romero-Romero, R.Vergara, G.Espinoza-Perez, A.Rodriguez-Romero, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.92 / 1.89
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	37.207, 57.656, 101.260, 90.00, 90.00, 90.00
R / Rfree (%)	15.9 / 21.2

The binding sites of Sodium atom in the Crystal Structure of the Periplasmic Lysine-, Arginine-, Ornithine- Binding Protein (Lao) R77A Mutant From Salmonella Typhimurium Complexed with Arginine (pdb code 6mlg). 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 the Periplasmic Lysine-, Arginine-, Ornithine- Binding Protein (Lao) R77A Mutant From Salmonella Typhimurium Complexed with Arginine, PDB code: 6mlg:

Sodium binding site 1 out of 1 in the Crystal Structure of the Periplasmic Lysine-, Arginine-, Ornithine- Binding Protein (Lao) R77A Mutant From Salmonella Typhimurium Complexed with Arginine


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 the Periplasmic Lysine-, Arginine-, Ornithine- Binding Protein (Lao) R77A Mutant From Salmonella Typhimurium Complexed with Arginine within 5.0Å range: probe atom residue distance (Å) B Occ E:Na305 b:39.5 occ:1.00 O E:HOH590 2.3 34.3 1.0 NH2 E:ARG218 2.4 38.9 1.0 O E:HOH548 2.5 36.6 1.0 NE E:ARG218 2.6 25.8 1.0 CZ E:ARG218 2.9 37.4 1.0 O E:HOH570 3.2 40.0 1.0 OH E:TYR236 3.6 26.7 1.0 CZ E:TYR236 3.8 22.3 1.0 CD E:ARG218 3.9 24.6 1.0 CE2 E:TYR236 4.0 23.0 1.0 NH1 E:ARG218 4.2 35.8 1.0 O E:HOH599 4.6 44.3 1.0 CE1 E:TYR236 4.6 22.1 1.0 O E:HOH585 4.6 22.8 1.0 CD2 E:TYR236 4.9 20.6 1.0 O E:HOH425 4.9 15.3 1.0 CB E:ARG218 4.9 18.1 1.0

R.Vergara, S.Romero-Romero, I.Velazquez-Lopez, G.Espinoza-Perez, A.Rodriguez-Hernandez, N.O.Pulido, A.Sosa-Peinado, A.Rodriguez-Romero, D.A.Fernandez-Velasco. The Interplay of Protein-Ligand and Water-Mediated Interactions Shape Affinity and Selectivity in the Lao Binding Protein. Febs J. 2019.
ISSN: ISSN 1742-464X
PubMed: 31348608
DOI: 10.1111/FEBS.15019