Potassium in PDB 1li9: Crystal Structure of Tem-34 Beta-Lactamase at 1.5 Angstrom

All present enzymatic activity of Crystal Structure of Tem-34 Beta-Lactamase at 1.5 Angstrom:
3.5.2.6;

The structure of Crystal Structure of Tem-34 Beta-Lactamase at 1.5 Angstrom, PDB code: 1li9 was solved by X.Wang, G.Minasov, B.K.Shoichet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	17.00 / 1.52
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	41.371, 59.604, 88.291, 90.00, 90.00, 90.00
R / Rfree (%)	17.7 / 18.9

The binding sites of Potassium atom in the Crystal Structure of Tem-34 Beta-Lactamase at 1.5 Angstrom (pdb code 1li9). 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 Tem-34 Beta-Lactamase at 1.5 Angstrom, PDB code: 1li9:

Potassium binding site 1 out of 1 in the Crystal Structure of Tem-34 Beta-Lactamase at 1.5 Angstrom


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 Tem-34 Beta-Lactamase at 1.5 Angstrom within 5.0Å range: probe atom residue distance (Å) B Occ A:K3 b:20.4 occ:0.50 O A:HOH653 2.5 34.1 1.0 O A:HOH355 2.7 22.0 1.0 O A:HOH652 2.9 39.0 1.0 N A:GLU63 2.9 13.1 1.0 CA A:GLU63 3.5 13.3 1.0 CD A:PRO62 3.5 12.1 1.0 N A:PRO62 3.6 12.9 1.0 CB A:GLU63 3.6 15.8 1.0 C A:GLU63 3.7 12.1 1.0 C A:ARG61 3.7 13.2 1.0 CG A:PRO62 3.7 11.8 1.0 N A:GLU64 3.8 11.0 1.0 CA A:ARG61 3.9 12.6 1.0 C A:PRO62 4.0 12.0 1.0 CG A:GLU64 4.1 14.6 1.0 CA A:PRO62 4.2 12.9 1.0 O A:GLU63 4.2 16.2 1.0 O A:ARG61 4.3 13.9 1.0 CG A:GLU63 4.5 17.2 1.0 O A:HOH411 4.5 14.7 0.4 O A:HOH593 4.5 45.6 1.0 CB A:PRO62 4.6 12.8 1.0 O A:HOH428 4.6 30.3 1.0 N A:ARG61 4.8 14.2 1.0 CA A:GLU64 4.8 13.0 1.0 O A:HOH411 4.9 17.4 0.6 CB A:GLU64 4.9 12.6 1.0 OE2 A:GLU64 4.9 19.1 1.0 CB A:ARG61 4.9 14.2 1.0

X.Wang, G.Minasov, B.K.Shoichet. The Structural Bases of Antibiotic Resistance in the Clinically Derived Mutant Beta-Lactamases Tem-30, Tem-32, and Tem-34. J.Biol.Chem. V. 277 32149 2002.
ISSN: ISSN 0021-9258
PubMed: 12058046
DOI: 10.1074/JBC.M204212200