Potassium in PDB 3nr6: Crystal Structure of Xenotropic Murine Leukemia Virus-Related Virus (Xmrv) Protease

The structure of Crystal Structure of Xenotropic Murine Leukemia Virus-Related Virus (Xmrv) Protease, PDB code: 3nr6 was solved by J.Lubkowski, M.Li, A.Gustchina, D.Zhou, Z.Dauter, A.Wlodawer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.97
Space group	P 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	63.915, 63.915, 106.509, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 23.3

The binding sites of Potassium atom in the Crystal Structure of Xenotropic Murine Leukemia Virus-Related Virus (Xmrv) Protease (pdb code 3nr6). 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 Crystal Structure of Xenotropic Murine Leukemia Virus-Related Virus (Xmrv) Protease, PDB code: 3nr6:

Potassium binding site 1 out of 1 in the Crystal Structure of Xenotropic Murine Leukemia Virus-Related Virus (Xmrv) Protease


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Xenotropic Murine Leukemia Virus-Related Virus (Xmrv) Protease within 5.0Å range: probe atom residue distance (Å) B Occ A:K126 b:45.6 occ:0.80 O A:HOH153 2.6 35.2 1.0 O A:GLN5 2.8 46.9 1.0 OE1 A:GLN8 2.8 42.4 1.0 O A:HOH139 2.9 33.8 1.0 O A:PRO26 3.0 40.8 1.0 C A:GLN5 3.7 45.2 1.0 CD A:GLN8 3.8 48.3 1.0 CB A:GLN5 3.8 42.9 1.0 C A:PRO26 3.8 38.4 1.0 CG A:GLN8 4.1 46.8 1.0 CA A:VAL27 4.2 36.2 1.0 N A:THR28 4.4 31.2 1.0 N A:VAL27 4.4 33.6 1.0 CA A:GLN5 4.4 44.0 1.0 CB A:GLN8 4.4 44.1 1.0 N A:GLY6 4.6 43.7 1.0 C A:VAL27 4.7 34.8 1.0 CG A:PRO26 4.8 49.9 1.0 CB A:PRO26 4.8 45.0 1.0 OG1 A:THR28 4.8 37.7 1.0 CA A:GLY6 4.8 52.8 1.0 CA A:PRO26 4.9 42.3 1.0

M.Li, F.Dimaio, D.Zhou, A.Gustchina, J.Lubkowski, Z.Dauter, D.Baker, A.Wlodawer. Crystal Structure of Xmrv Protease Differs From the Structures of Other Retropepsins. Nat.Struct.Mol.Biol. V. 18 227 2011.
ISSN: ISSN 1545-9993
PubMed: 21258323
DOI: 10.1038/NSMB.1964