Potassium in PDB 1pi5: Structure of N289A Mutant of Ampc in Complex with SM2, Carboxyphenylglycylboronic Acid Bearing the Cephalothin R1 Side Chain

All present enzymatic activity of Structure of N289A Mutant of Ampc in Complex with SM2, Carboxyphenylglycylboronic Acid Bearing the Cephalothin R1 Side Chain:
3.5.2.6;

The structure of Structure of N289A Mutant of Ampc in Complex with SM2, Carboxyphenylglycylboronic Acid Bearing the Cephalothin R1 Side Chain, PDB code: 1pi5 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)	15.00 / 1.49
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	119.050, 76.008, 97.595, 90.00, 115.54, 90.00
R / Rfree (%)	15.5 / 16.8

The binding sites of Potassium atom in the Structure of N289A Mutant of Ampc in Complex with SM2, Carboxyphenylglycylboronic Acid Bearing the Cephalothin R1 Side Chain (pdb code 1pi5). 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 SM2, Carboxyphenylglycylboronic Acid Bearing the Cephalothin R1 Side Chain, PDB code: 1pi5:
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 SM2, Carboxyphenylglycylboronic 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 SM2, Carboxyphenylglycylboronic Acid Bearing the Cephalothin R1 Side Chain within 5.0Å range: probe atom residue distance (Å) B Occ A:K2 b:19.2 occ:0.60 O A:HOH832 2.6 35.0 1.0 O A:HOH522 2.7 25.2 1.0 OD1 A:ASP217 2.8 11.8 1.0 O A:GLY214 3.0 12.6 1.0 O A:HOH569 3.0 23.4 1.0 O A:HOH829 3.1 50.9 1.0 O A:HOH702 3.3 34.4 1.0 CG A:ASP217 3.6 12.5 1.0 O A:HOH828 3.8 41.1 1.0 C A:GLY214 4.0 12.3 1.0 N A:LEU216 4.0 10.6 1.0 OD2 A:ASP217 4.0 14.0 1.0 CA A:ALA215 4.1 11.9 1.0 N A:ASP217 4.2 11.2 1.0 O A:HOH483 4.3 20.0 1.0 O A:HOH982 4.4 44.4 1.0 C A:ALA215 4.4 11.2 1.0 N A:ALA215 4.5 11.7 1.0 CB A:ASP217 4.8 11.0 1.0 CA A:LEU216 4.8 10.3 1.0 O A:HOH713 4.8 31.0 1.0 N A:GLY214 4.9 12.1 1.0

Potassium binding site 2 out of 2 in the Structure of N289A Mutant of Ampc in Complex with SM2, Carboxyphenylglycylboronic 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 SM2, Carboxyphenylglycylboronic Acid Bearing the Cephalothin R1 Side Chain within 5.0Å range: probe atom residue distance (Å) B Occ B:K3 b:17.1 occ:0.60 O B:HOH486 2.8 21.3 1.0 O B:HOH536 2.9 26.7 1.0 O B:GLY214 2.9 12.7 1.0 OD1 B:ASP217 2.9 12.2 1.0 O B:HOH611 2.9 27.2 1.0 O B:HOH488 3.0 19.6 1.0 CG B:ASP217 3.6 11.5 1.0 N B:LEU216 3.8 12.4 1.0 C B:GLY214 3.8 11.7 1.0 CA B:ALA215 4.0 14.0 1.0 OD2 B:ASP217 4.0 13.9 1.0 O B:HOH634 4.1 30.5 1.0 N B:ASP217 4.1 10.1 1.0 C B:ALA215 4.2 11.8 1.0 N B:ALA215 4.3 12.8 1.0 O B:HOH935 4.5 45.8 1.0 O B:HOH647 4.6 27.3 1.0 CA B:LEU216 4.6 12.2 1.0 CB B:ASP217 4.7 11.6 1.0 O B:HOH529 4.8 29.3 1.0 N B:GLY214 4.8 13.0 1.0 C B:LEU216 4.9 11.3 1.0 CA B:ASP217 5.0 9.6 1.0 CA B:GLY214 5.0 13.6 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