Potassium in PDB 1li0: Crystal Structure of Tem-32 Beta-Lactamase at 1.6 Angstrom

All present enzymatic activity of Crystal Structure of Tem-32 Beta-Lactamase at 1.6 Angstrom:
3.5.2.6;

The structure of Crystal Structure of Tem-32 Beta-Lactamase at 1.6 Angstrom, PDB code: 1li0 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 / 1.61
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	41.222, 60.504, 88.712, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 21.7

The binding sites of Potassium atom in the Crystal Structure of Tem-32 Beta-Lactamase at 1.6 Angstrom (pdb code 1li0). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of Tem-32 Beta-Lactamase at 1.6 Angstrom, PDB code: 1li0:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of Tem-32 Beta-Lactamase at 1.6 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-32 Beta-Lactamase at 1.6 Angstrom within 5.0Å range: probe atom residue distance (Å) B Occ A:K2 b:20.9 occ:0.50 O A:HOH581 2.6 35.7 0.5 O A:HOH583 2.7 47.0 1.0 OD1 A:ASP233 2.7 25.7 1.0 O A:MET211 2.8 15.2 1.0 O A:ASP233 2.9 17.8 1.0 O A:ALA213 3.2 41.7 1.0 O A:HOH581 3.6 30.9 0.5 C A:MET211 3.7 17.8 1.0 C A:ASP233 3.7 15.4 1.0 NH2 A:ARG222 3.8 29.3 1.0 CG A:ASP233 3.8 23.0 1.0 CA A:MET211 4.2 16.7 1.0 N A:ASP233 4.3 15.1 1.0 C A:ALA213 4.4 40.0 1.0 NE A:ARG222 4.4 28.9 1.0 CA A:ASP233 4.4 16.8 1.0 CZ A:ARG222 4.5 32.6 1.0 O A:TRP210 4.5 20.1 1.0 O A:HOH337 4.5 30.9 1.0 OD2 A:ASP233 4.6 23.7 1.0 N A:LYS234 4.6 14.4 1.0 N A:GLU212 4.7 18.6 1.0 CB A:ALA217 4.7 50.8 1.0 CB A:ASP233 4.7 16.7 1.0 C A:GLU212 4.8 26.1 1.0 CA A:LYS234 4.8 14.0 1.0 N A:ALA213 4.8 29.9 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of Tem-32 Beta-Lactamase at 1.6 Angstrom


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of Tem-32 Beta-Lactamase at 1.6 Angstrom within 5.0Å range: probe atom residue distance (Å) B Occ A:K3 b:27.4 occ:0.65 ND2 A:ASN100 2.1 33.1 0.3 OD1 A:ASN100 2.3 32.7 0.3 CG A:ASN100 2.5 30.7 0.3 OD1 A:ASP101 3.1 19.4 1.0 O A:HOH360 3.8 15.1 1.0 CG A:ASP101 3.8 22.6 1.0 CB A:ASN100 3.9 29.6 0.7 O A:ASN100 3.9 27.6 0.3 CB A:ASN100 4.0 30.4 0.3 O A:ASN100 4.0 28.3 0.7 C A:ASN100 4.1 27.1 0.3 O A:HOH586 4.1 20.9 1.0 C A:ASN100 4.1 27.2 0.7 OD2 A:ASP101 4.2 21.0 1.0 N A:ASP101 4.4 24.1 1.0 O A:HOH330 4.4 25.6 1.0 CA A:ASP101 4.5 23.5 1.0 O A:HOH325 4.6 20.8 1.0 CA A:ASN100 4.7 29.0 0.7 CA A:ASN100 4.7 28.9 0.3 CB A:ASP101 4.8 21.1 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