Potassium in PDB 3fkv: Ampc K67R Mutant Complexed with Benzo(B)Thiophene-2-Boronic Acid (Bzb)

All present enzymatic activity of Ampc K67R Mutant Complexed with Benzo(B)Thiophene-2-Boronic Acid (Bzb):
3.5.2.6;

The structure of Ampc K67R Mutant Complexed with Benzo(B)Thiophene-2-Boronic Acid (Bzb), PDB code: 3fkv was solved by Y.Chen, A.Mcreynolds, B.K.Shoichet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	87.71 / 1.85
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	118.043, 76.949, 97.831, 90.00, 116.23, 90.00
R / Rfree (%)	16.3 / 20.3

The binding sites of Potassium atom in the Ampc K67R Mutant Complexed with Benzo(B)Thiophene-2-Boronic Acid (Bzb) (pdb code 3fkv). 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 Ampc K67R Mutant Complexed with Benzo(B)Thiophene-2-Boronic Acid (Bzb), PDB code: 3fkv:

Potassium binding site 1 out of 1 in the Ampc K67R Mutant Complexed with Benzo(B)Thiophene-2-Boronic Acid (Bzb)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Ampc K67R Mutant Complexed with Benzo(B)Thiophene-2-Boronic Acid (Bzb) within 5.0Å range: probe atom residue distance (Å) B Occ B:K502 b:22.8 occ:1.00 O B:HOH458 2.9 26.1 1.0 O A:HOH625 3.1 23.8 1.0 O B:HOH672 3.6 24.4 1.0 CA A:PRO303 3.6 13.9 1.0 CD A:PRO304 3.7 14.2 1.0 CG2 B:THR302 3.8 16.5 1.0 CA B:PRO303 3.8 13.4 1.0 CA B:THR302 3.9 14.7 1.0 CG2 A:THR302 4.0 16.2 1.0 O A:HOH475 4.0 20.7 0.5 CA A:THR302 4.1 13.8 1.0 CD B:PRO304 4.1 12.6 1.0 CB A:PRO303 4.1 13.9 1.0 CB B:THR302 4.3 14.8 1.0 O B:ILE301 4.3 11.4 1.0 O A:ILE301 4.3 12.3 1.0 OG1 B:THR302 4.4 18.4 1.0 CB A:THR302 4.4 14.6 1.0 N B:PRO303 4.5 13.5 1.0 N A:PRO303 4.5 13.5 1.0 N A:PRO304 4.5 14.7 1.0 CB B:PRO303 4.5 13.5 1.0 OG1 A:THR302 4.6 16.8 1.0 C A:PRO303 4.6 13.7 1.0 C B:THR302 4.6 13.3 1.0 C A:THR302 4.7 13.3 1.0 CG A:PRO304 4.7 14.8 1.0 C B:PRO303 4.8 12.4 1.0 N B:PRO304 4.8 13.6 1.0 O B:HOH483 4.8 25.3 1.0 O A:HOH439 4.9 35.7 1.0 CG B:PRO304 4.9 14.5 1.0 N B:THR302 5.0 13.0 1.0

Y.Chen, A.Mcreynolds, B.K.Shoichet. Re-Examining the Role of LYS67 in Class C Beta-Lactamase Catalysis. Protein Sci. V. 18 662 2009.
ISSN: ISSN 0961-8368
PubMed: 19241376
DOI: 10.1002/PRO.60