Potassium in PDB 2ffy: Ampc Beta-Lactamase N289A Mutant in Complex with A Boronic Acid Deacylation Transition State Analog Compound SM3

All present enzymatic activity of Ampc Beta-Lactamase N289A Mutant in Complex with A Boronic Acid Deacylation Transition State Analog Compound SM3:
3.5.2.6;

The structure of Ampc Beta-Lactamase N289A Mutant in Complex with A Boronic Acid Deacylation Transition State Analog Compound SM3, PDB code: 2ffy was solved by Y.Chen, G.Minasov, T.A.Roth, F.Prati, B.K.Shoichet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 1.07
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	118.840, 76.063, 97.898, 90.00, 115.85, 90.00
R / Rfree (%)	13.3 / 16.4

The binding sites of Potassium atom in the Ampc Beta-Lactamase N289A Mutant in Complex with A Boronic Acid Deacylation Transition State Analog Compound SM3 (pdb code 2ffy). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Ampc Beta-Lactamase N289A Mutant in Complex with A Boronic Acid Deacylation Transition State Analog Compound SM3, PDB code: 2ffy:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Ampc Beta-Lactamase N289A Mutant in Complex with A Boronic Acid Deacylation Transition State Analog Compound SM3


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Ampc Beta-Lactamase N289A Mutant in Complex with A Boronic Acid Deacylation Transition State Analog Compound SM3 within 5.0Å range: probe atom residue distance (Å) B Occ A:K2 b:18.6 occ:0.36 O A:HOH5860 2.5 45.2 1.0 O A:HOH5425 2.6 26.4 1.0 OD1 A:ASP217 2.7 13.1 1.0 O A:HOH5829 2.9 39.9 1.0 O A:GLY214 3.0 14.0 1.0 O A:HOH5862 3.1 51.0 1.0 O A:HOH5553 3.1 23.9 1.0 H A:ASP217 3.4 13.7 1.0 H A:LEU216 3.4 15.4 1.0 HA A:ALA215 3.5 16.9 1.0 CG A:ASP217 3.6 12.2 1.0 O A:HOH5910 3.8 40.0 1.0 N A:LEU216 3.9 12.9 1.0 O A:HOH5909 4.0 38.6 0.5 C A:GLY214 4.0 13.8 1.0 OD2 A:ASP217 4.0 14.4 1.0 H A:ALA218 4.1 14.0 1.0 N A:ASP217 4.2 11.4 1.0 CA A:ALA215 4.2 14.1 1.0 O A:HOH5505 4.3 24.8 1.0 H A:GLY214 4.4 17.7 1.0 C A:ALA215 4.4 12.8 1.0 N A:ALA215 4.6 13.8 1.0 HA A:LEU216 4.6 14.2 1.0 CB A:ASP217 4.7 12.1 1.0 CA A:LEU216 4.7 11.8 1.0 O A:HOH5714 4.8 32.7 1.0 O A:HOH5756 4.8 32.8 1.0 HB3 A:ASP217 4.9 14.5 1.0 C A:LEU216 5.0 10.9 1.0 N A:GLY214 5.0 14.7 1.0 CA A:ASP217 5.0 11.1 1.0 N A:ALA218 5.0 11.7 1.0

Potassium binding site 2 out of 2 in the Ampc Beta-Lactamase N289A Mutant in Complex with A Boronic Acid Deacylation Transition State Analog Compound SM3


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Ampc Beta-Lactamase N289A Mutant in Complex with A Boronic Acid Deacylation Transition State Analog Compound SM3 within 5.0Å range: probe atom residue distance (Å) B Occ B:K3 b:11.0 occ:0.36 O B:HOH9407 2.7 19.0 1.0 O B:GLY214 2.8 12.5 1.0 O B:HOH9478 2.8 10.5 0.5 OD1 B:ASP217 2.9 12.1 1.0 O B:HOH9548 2.9 25.6 1.0 O B:HOH9546 2.9 29.1 1.0 H B:LEU216 3.2 13.7 1.0 HA B:ALA215 3.2 15.5 1.0 H B:ASP217 3.3 12.7 1.0 CG B:ASP217 3.7 11.6 1.0 N B:LEU216 3.7 11.4 1.0 C B:GLY214 3.8 12.1 1.0 CA B:ALA215 4.0 12.9 1.0 N B:ASP217 4.1 10.6 1.0 O B:HOH9634 4.1 17.6 0.5 OD2 B:ASP217 4.1 12.9 1.0 C B:ALA215 4.2 11.3 1.0 H B:ALA218 4.2 12.8 1.0 N B:ALA215 4.3 12.7 1.0 H B:GLY214 4.3 16.3 1.0 HA B:LEU216 4.4 13.6 1.0 CA B:LEU216 4.6 11.3 1.0 O B:HOH9617 4.6 30.4 1.0 O B:HOH9591 4.7 34.3 1.0 CB B:ASP217 4.7 11.0 1.0 C B:LEU216 4.8 9.8 1.0 O B:HOH9527 4.9 15.3 0.5 HB3 B:ASP217 4.9 13.2 1.0 N B:GLY214 4.9 13.6 1.0 CA B:ASP217 4.9 10.2 1.0 CA B:GLY214 5.0 14.0 1.0

Y.Chen, G.Minasov, T.A.Roth, F.Prati, B.K.Shoichet. The Deacylation Mechanism of Ampc Beta-Lactamase at Ultrahigh Resolution J.Am.Chem.Soc. V. 128 2970 2006.
ISSN: ISSN 0002-7863
PubMed: 16506777
DOI: 10.1021/JA056806M