Potassium in PDB 6n5o: Structure of Human Pir-Mirna-202 Apical Loop and One-Base-Pair Fused to the Ydao Riboswitch Scaffold

The structure of Structure of Human Pir-Mirna-202 Apical Loop and One-Base-Pair Fused to the Ydao Riboswitch Scaffold, PDB code: 6n5o was solved by G.M.Shoffner, Z.Peng, F.Guo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	99.52 / 2.71
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	114.920, 114.920, 115.330, 90.00, 90.00, 120.00
R / Rfree (%)	18 / 21.9

The structure of Structure of Human Pir-Mirna-202 Apical Loop and One-Base-Pair Fused to the Ydao Riboswitch Scaffold also contains other interesting chemical elements:

Magnesium

(Mg)

4 atoms

The binding sites of Potassium atom in the Structure of Human Pir-Mirna-202 Apical Loop and One-Base-Pair Fused to the Ydao Riboswitch Scaffold (pdb code 6n5o). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Structure of Human Pir-Mirna-202 Apical Loop and One-Base-Pair Fused to the Ydao Riboswitch Scaffold, PDB code: 6n5o:

Potassium binding site 1 out of 1 in the Structure of Human Pir-Mirna-202 Apical Loop and One-Base-Pair Fused to the Ydao Riboswitch Scaffold


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of Human Pir-Mirna-202 Apical Loop and One-Base-Pair Fused to the Ydao Riboswitch Scaffold within 5.0Å range: probe atom residue distance (Å) B Occ A:K205 b:0.2 occ:1.00 O2' A:GTP1 3.4 79.4 1.0 O3' A:GTP1 3.5 65.7 1.0 OP1 A:G2 3.9 88.3 1.0 O2' A:U11 3.9 85.6 1.0 O2 A:U11 4.1 95.1 1.0 C5' A:G2 4.1 76.2 1.0 O4' A:C12 4.3 94.5 1.0 P A:G2 4.3 94.8 1.0 C2' A:GTP1 4.4 77.5 1.0 C1' A:C12 4.4 95.9 1.0 C3' A:GTP1 4.5 78.7 1.0 O2' A:C12 4.7 0.3 1.0 C2' A:U11 4.7 77.1 1.0 O5' A:G2 4.7 78.2 1.0 C1' A:A25 4.9 83.8 1.0

G.M.Shoffner, Z.Peng, F.Guo. Three-Dimensional Structures of Pri-Mirna Apical Junctions and Loops Revealed By Scaffold-Directed Crystallography To Be Published.