Potassium in PDB 1o07: Crystal Structure of the Complex Between Q120L/Y150E Mutant of Ampc and A Beta-Lactam Inhibitor (Mxg)

All present enzymatic activity of Crystal Structure of the Complex Between Q120L/Y150E Mutant of Ampc and A Beta-Lactam Inhibitor (Mxg):
3.5.2.6;

The structure of Crystal Structure of the Complex Between Q120L/Y150E Mutant of Ampc and A Beta-Lactam Inhibitor (Mxg), PDB code: 1o07 was solved by S.O.Meroueh, G.Minasov, W.Lee, B.K.Shoichet, S.Mobashery, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.77 / 1.71
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	118.808, 76.298, 98.127, 90.00, 116.21, 90.00
R / Rfree (%)	15.4 / 19.1

The binding sites of Potassium atom in the Crystal Structure of the Complex Between Q120L/Y150E Mutant of Ampc and A Beta-Lactam Inhibitor (Mxg) (pdb code 1o07). 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 the Complex Between Q120L/Y150E Mutant of Ampc and A Beta-Lactam Inhibitor (Mxg), PDB code: 1o07:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of the Complex Between Q120L/Y150E Mutant of Ampc and A Beta-Lactam Inhibitor (Mxg)


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 the Complex Between Q120L/Y150E Mutant of Ampc and A Beta-Lactam Inhibitor (Mxg) within 5.0Å range: probe atom residue distance (Å) B Occ A:K2 b:42.8 occ:1.00 O A:HOH470 3.0 29.6 1.0 OD1 A:ASP217 3.0 8.9 1.0 O A:HOH726 3.1 48.4 1.0 O A:GLY214 3.2 8.2 1.0 O A:HOH450 3.2 35.2 1.0 O A:HOH620 3.3 38.8 0.5 O A:HOH552 3.6 45.2 1.0 CG A:ASP217 3.8 12.2 1.0 OD2 A:ASP217 4.1 8.1 1.0 C A:GLY214 4.2 10.4 1.0 N A:LEU216 4.2 7.0 1.0 O A:HOH448 4.4 29.0 1.0 CA A:ALA215 4.5 9.9 1.0 N A:ASP217 4.5 8.2 1.0 C A:ALA215 4.7 8.8 1.0 N A:ALA215 4.7 9.6 1.0 O A:HOH708 4.9 34.5 1.0 CB A:ASP217 5.0 7.3 1.0 CA A:LEU216 5.0 8.8 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of the Complex Between Q120L/Y150E Mutant of Ampc and A Beta-Lactam Inhibitor (Mxg)


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 the Complex Between Q120L/Y150E Mutant of Ampc and A Beta-Lactam Inhibitor (Mxg) within 5.0Å range: probe atom residue distance (Å) B Occ B:K1 b:40.4 occ:1.00 O B:HOH559 2.7 39.0 1.0 O B:HOH445 2.8 27.1 1.0 O B:HOH475 3.0 32.8 1.0 O B:GLY214 3.1 9.6 1.0 OD1 B:ASP217 3.1 11.8 1.0 O B:HOH543 3.6 28.5 0.6 CG B:ASP217 3.9 12.9 1.0 O B:HOH543 4.1 19.6 0.4 C B:GLY214 4.1 11.5 1.0 N B:LEU216 4.1 10.3 1.0 OD2 B:ASP217 4.2 12.1 1.0 N B:ASP217 4.4 8.8 1.0 CA B:ALA215 4.4 11.2 1.0 N B:ALA215 4.6 10.2 1.0 O B:HOH477 4.6 27.6 1.0 C B:ALA215 4.7 9.6 1.0 CA B:LEU216 4.9 10.6 1.0 O B:HOH726 4.9 40.0 1.0

S.O.Meroueh, G.Minasov, W.Lee, B.K.Shoichet, S.Mobashery. Structural Aspects For Evolution of Beta-Lactamases From Penicillin-Binding Proteins J.Am.Chem.Soc. V. 125 9612 2003.
ISSN: ISSN 0002-7863
PubMed: 12904027
DOI: 10.1021/JA034861U