Sodium in PDB 5mss: Structure of the A-Pcp Didomain of Carboxylic Acid Reductase (Car) From Segniliparus Rugosus in Complex with Amp

The structure of Structure of the A-Pcp Didomain of Carboxylic Acid Reductase (Car) From Segniliparus Rugosus in Complex with Amp, PDB code: 5mss was solved by D.Gahloth, D.Leys, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	106.12 / 1.96
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	59.719, 127.693, 212.244, 90.00, 90.00, 90.00
R / Rfree (%)	20.4 / 25.4

The binding sites of Sodium atom in the Structure of the A-Pcp Didomain of Carboxylic Acid Reductase (Car) From Segniliparus Rugosus in Complex with Amp (pdb code 5mss). 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 Structure of the A-Pcp Didomain of Carboxylic Acid Reductase (Car) From Segniliparus Rugosus in Complex with Amp, PDB code: 5mss:

Sodium binding site 1 out of 1 in the Structure of the A-Pcp Didomain of Carboxylic Acid Reductase (Car) From Segniliparus Rugosus in Complex with Amp


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of the A-Pcp Didomain of Carboxylic Acid Reductase (Car) From Segniliparus Rugosus in Complex with Amp within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1202 b:36.1 occ:1.00 N A:GLU533 2.8 18.1 1.0 O A:GLU533 2.8 19.6 1.0 OE1 A:GLN531 2.9 19.9 1.0 O A:LEU529 3.2 19.1 1.0 N A:LEU529 3.2 18.4 1.0 N A:GLY532 3.3 16.1 1.0 C A:LEU529 3.4 19.5 1.0 CB A:LEU529 3.4 19.7 1.0 CB A:GLN531 3.4 20.1 1.0 CA A:LEU529 3.5 19.4 1.0 N A:GLN531 3.5 18.1 1.0 CA A:GLU533 3.5 20.4 1.0 C A:GLU533 3.6 19.4 1.0 CA A:GLN531 3.7 18.4 1.0 CB A:GLU533 3.7 23.4 1.0 C A:GLN531 3.7 17.5 1.0 C A:GLY532 3.8 21.6 1.0 CD A:GLN531 3.9 22.1 1.0 CA A:GLY532 4.0 21.1 1.0 N A:SER530 4.2 17.7 1.0 CG A:GLN531 4.2 21.5 1.0 CG A:LEU529 4.3 19.9 1.0 C A:LYS528 4.4 15.9 1.0 CG A:GLU533 4.4 29.0 1.0 C A:SER530 4.5 17.7 1.0 O A:GLN531 4.6 18.4 1.0 CE1 A:TYR604 4.6 37.1 1.0 CA A:LYS528 4.8 15.2 1.0 CZ A:TYR604 4.8 36.7 1.0 CA A:SER530 4.9 16.2 1.0 CD1 A:LEU529 4.9 20.0 1.0 N A:PHE534 4.9 17.6 1.0 CG1 A:VAL535 4.9 31.9 1.0 O A:GLY532 4.9 20.2 1.0 CD1 A:TYR604 5.0 35.9 1.0

D.Gahloth, M.S.Dunstan, D.Quaglia, E.Klumbys, M.P.Lockhart-Cairns, A.M.Hill, S.R.Derrington, N.S.Scrutton, N.J.Turner, D.Leys. Structures of Carboxylic Acid Reductase Reveal Domain Dynamics Underlying Catalysis. Nat. Chem. Biol. V. 13 975 2017.
ISSN: ESSN 1552-4469
PubMed: 28719588
DOI: 10.1038/NCHEMBIO.2434