Potassium in PDB 1pi4: Structure of N289A Mutant of Ampc in Complex with SM3, A Phenylglyclboronic Acid Bearing the Cephalothin R1 Side Chain

All present enzymatic activity of Structure of N289A Mutant of Ampc in Complex with SM3, A Phenylglyclboronic Acid Bearing the Cephalothin R1 Side Chain:
3.5.2.6;

The structure of Structure of N289A Mutant of Ampc in Complex with SM3, A Phenylglyclboronic Acid Bearing the Cephalothin R1 Side Chain, PDB code: 1pi4 was solved by T.A.Roth, G.Minasov, P.J.Focia, B.K.Shoichet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.39
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	118.628, 76.104, 97.836, 90.00, 115.61, 90.00
R / Rfree (%)	15.9 / 17.3

The binding sites of Potassium atom in the Structure of N289A Mutant of Ampc in Complex with SM3, A Phenylglyclboronic Acid Bearing the Cephalothin R1 Side Chain (pdb code 1pi4). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of N289A Mutant of Ampc in Complex with SM3, A Phenylglyclboronic Acid Bearing the Cephalothin R1 Side Chain, PDB code: 1pi4:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Structure of N289A Mutant of Ampc in Complex with SM3, A Phenylglyclboronic Acid Bearing the Cephalothin R1 Side Chain


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of N289A Mutant of Ampc in Complex with SM3, A Phenylglyclboronic Acid Bearing the Cephalothin R1 Side Chain within 5.0Å range: probe atom residue distance (Å) B Occ A:K2 b:18.8 occ:0.50 O A:HOH711 2.3 28.3 0.5 O A:HOH522 2.6 25.3 1.0 O A:HOH863 2.7 35.9 1.0 OD1 A:ASP217 2.8 12.1 1.0 O A:GLY214 2.9 12.6 1.0 O A:HOH569 3.0 23.3 1.0 O A:HOH860 3.2 45.2 1.0 O A:HOH711 3.4 27.9 0.5 CG A:ASP217 3.6 10.8 1.0 O A:HOH859 3.9 43.3 1.0 N A:LEU216 3.9 11.7 1.0 C A:GLY214 3.9 12.6 1.0 OD2 A:ASP217 4.0 13.7 1.0 N A:ASP217 4.1 11.7 1.0 CA A:ALA215 4.1 12.9 1.0 C A:ALA215 4.4 10.6 1.0 O A:HOH483 4.4 22.3 1.0 N A:ALA215 4.5 12.6 1.0 CA A:LEU216 4.7 11.4 1.0 O A:HOH728 4.7 30.1 1.0 CB A:ASP217 4.7 10.7 1.0 N A:GLY214 4.9 12.4 1.0 C A:LEU216 4.9 11.4 1.0 CA A:ASP217 5.0 10.6 1.0 N A:ALA218 5.0 10.4 1.0

Potassium binding site 2 out of 2 in the Structure of N289A Mutant of Ampc in Complex with SM3, A Phenylglyclboronic Acid Bearing the Cephalothin R1 Side Chain


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of N289A Mutant of Ampc in Complex with SM3, A Phenylglyclboronic Acid Bearing the Cephalothin R1 Side Chain within 5.0Å range: probe atom residue distance (Å) B Occ B:K3 b:13.5 occ:0.50 O B:HOH486 2.6 20.7 1.0 O B:HOH778 2.7 42.9 1.0 O B:HOH488 2.8 18.5 1.0 O B:HOH536 2.9 23.1 1.0 OD1 B:ASP217 2.9 12.3 1.0 O B:GLY214 3.0 12.6 1.0 O B:HOH612 3.0 25.5 1.0 CG B:ASP217 3.7 10.7 1.0 N B:LEU216 3.8 11.8 1.0 C B:GLY214 4.0 11.2 1.0 CA B:ALA215 4.1 12.9 1.0 OD2 B:ASP217 4.1 12.9 1.0 N B:ASP217 4.1 10.0 1.0 O B:HOH635 4.2 30.6 1.0 C B:ALA215 4.3 11.4 1.0 N B:ALA215 4.5 12.0 1.0 O B:HOH528 4.6 30.1 1.0 O B:HOH650 4.6 28.8 1.0 CA B:LEU216 4.6 10.9 1.0 O B:HOH882 4.7 45.3 1.0 CB B:ASP217 4.8 9.8 1.0 O B:HOH532 4.9 23.4 1.0 C B:LEU216 4.9 10.7 1.0 O B:HOH751 5.0 24.5 1.0 N B:GLY214 5.0 12.3 1.0

T.A.Roth, G.Minasov, S.Morandi, F.Prati, B.K.Shoichet. Thermodynamic Cycle Analysis and Inhibitor Design Against Beta-Lactamase. Biochemistry V. 42 14483 2003.
ISSN: ISSN 0006-2960
PubMed: 14661960
DOI: 10.1021/BI035054A