Potassium in PDB 5jgz: Spin-Labeled T4 Lysozyme Construct T151V1

All present enzymatic activity of Spin-Labeled T4 Lysozyme Construct T151V1:
3.2.1.17;

The structure of Spin-Labeled T4 Lysozyme Construct T151V1, PDB code: 5jgz was solved by A.R.Balo, H.Feyrer, O.P.Ernst, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.73 / 1.53
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	59.460, 59.460, 95.302, 90.00, 90.00, 120.00
R / Rfree (%)	16.7 / 19.5

The structure of Spin-Labeled T4 Lysozyme Construct T151V1 also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Potassium atom in the Spin-Labeled T4 Lysozyme Construct T151V1 (pdb code 5jgz). 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 Spin-Labeled T4 Lysozyme Construct T151V1, PDB code: 5jgz:

Potassium binding site 1 out of 1 in the Spin-Labeled T4 Lysozyme Construct T151V1


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Spin-Labeled T4 Lysozyme Construct T151V1 within 5.0Å range: probe atom residue distance (Å) B Occ A:K202 b:23.6 occ:1.00 O A:HOH418 2.6 33.3 1.0 O A:HOH494 2.8 29.7 1.0 O A:HOH393 2.9 17.1 1.0 O A:GLU11 2.9 14.0 1.0 OE1 A:GLU11 3.0 16.2 1.0 OH A:TYR18 3.0 21.1 1.0 O A:HOH338 3.0 30.4 1.0 O A:HOH440 3.5 25.2 1.0 O A:HOH490 3.5 33.1 1.0 O A:HOH302 3.8 23.5 1.0 C A:GLU11 3.8 11.2 1.0 CA A:GLU11 3.9 11.6 1.0 CZ A:TYR18 3.9 17.5 1.0 CE2 A:TYR18 3.9 16.6 1.0 CD A:GLU11 4.2 15.1 1.0 CB A:GLU11 4.3 11.8 1.0 CA A:GLY30 4.4 12.2 1.0 O A:HOH507 4.6 34.0 1.0 O A:HOH483 4.7 27.6 1.0 N A:GLY30 4.7 10.8 1.0 CG A:GLU11 4.9 12.2 1.0 O A:ASP10 4.9 15.4 1.0 CB A:ASP20 4.9 13.6 1.0

A.R.Balo, H.Feyrer, O.P.Ernst. Toward Precise Interpretation of Deer-Based Distance Distributions: Insights From Structural Characterization of V1 Spin-Labeled Side Chains. Biochemistry V. 55 5256 2016.
ISSN: ISSN 1520-4995
PubMed: 27532325
DOI: 10.1021/ACS.BIOCHEM.6B00608