Potassium in PDB 1p2l: T4 Lysozyme Core Repacking Mutant V87I/Ta

All present enzymatic activity of T4 Lysozyme Core Repacking Mutant V87I/Ta:
3.2.1.17;

The structure of T4 Lysozyme Core Repacking Mutant V87I/Ta, PDB code: 1p2l was solved by B.H.Mooers, D.Datta, W.A.Baase, E.S.Zollars, S.L.Mayo, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.70 / 1.58
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	59.643, 59.643, 95.357, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The structure of T4 Lysozyme Core Repacking Mutant V87I/Ta also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Potassium atom in the T4 Lysozyme Core Repacking Mutant V87I/Ta (pdb code 1p2l). 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 T4 Lysozyme Core Repacking Mutant V87I/Ta, PDB code: 1p2l:

Potassium binding site 1 out of 1 in the T4 Lysozyme Core Repacking Mutant V87I/Ta


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of T4 Lysozyme Core Repacking Mutant V87I/Ta within 5.0Å range: probe atom residue distance (Å) B Occ A:K972 b:15.3 occ:0.77 O A:GLU11 2.9 10.7 1.0 OH A:TYR18 3.0 20.3 1.0 O A:HOH204 3.0 12.5 1.0 O A:HOH304 3.0 26.4 1.0 O A:HOH207 3.0 22.6 1.0 O A:HOH502 3.0 38.6 1.0 OE2 A:GLU11 3.1 13.7 1.0 O A:HOH405 3.4 21.2 1.0 C A:GLU11 3.8 7.9 1.0 CA A:GLU11 3.9 8.7 1.0 O A:HOH285 3.9 24.8 1.0 CZ A:TYR18 4.0 17.5 1.0 CE1 A:TYR18 4.0 16.5 1.0 CB A:GLU11 4.3 10.1 1.0 CD A:GLU11 4.3 16.1 1.0 CA A:GLY30 4.5 7.8 1.0 N A:GLY30 4.7 6.9 1.0 O A:HOH236 4.7 25.9 1.0 O A:ASP10 4.9 11.9 1.0 CG A:GLU11 4.9 9.8 1.0 CB A:ASP20 4.9 8.4 1.0 O A:HOH531 5.0 32.3 1.0

B.H.Mooers, D.Datta, W.A.Baase, E.S.Zollars, S.L.Mayo, B.W.Matthews. Repacking the Core of T4 Lysozyme By Automated Design J.Mol.Biol. V. 332 741 2003.
ISSN: ISSN 0022-2836
PubMed: 12963380
DOI: 10.1016/S0022-2836(03)00856-8