Potassium in PDB 9gl0: Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila

The structure of Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila, PDB code: 9gl0 was solved by L.G.Graf, S.Schulze, G.J.Palm, M.Lammers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.96 / 2.70
Space group	P 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	109.121, 109.121, 400.511, 90, 90, 90
R / Rfree (%)	24 / 31.6

The structure of Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila also contains other interesting chemical elements:

Zinc

(Zn)

4 atoms

The binding sites of Potassium atom in the Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila (pdb code 9gl0). 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 Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila, PDB code: 9gl0:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila


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 Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila within 5.0Å range: probe atom residue distance (Å) B Occ A:K502 b:100.4 occ:1.00 O A:ASP219 2.6 99.3 1.0 O A:VAL244 2.7 103.4 1.0 OD1 A:ASP243 2.8 100.4 1.0 O A:GLY217 2.8 94.7 1.0 OD1 A:ASP223 2.9 109.7 1.0 O A:ASN221 3.1 94.8 1.0 CG A:ASP223 3.5 99.7 1.0 C A:GLY217 3.6 97.8 1.0 C A:ASP219 3.7 94.1 1.0 OD2 A:ASP223 3.7 95.8 1.0 C A:VAL244 3.8 100.5 1.0 N A:ASP223 3.9 95.2 1.0 CG A:ASP243 4.0 102.2 1.0 N A:ASP219 4.0 94.2 1.0 C A:ASN221 4.0 96.9 1.0 N A:VAL244 4.1 101.8 1.0 CA A:ASP219 4.2 90.6 1.0 CA A:ARG222 4.2 95.6 1.0 CB A:ASP219 4.3 95.0 1.0 CB A:PHE245 4.3 99.0 1.0 C A:ARG222 4.4 99.4 1.0 C A:THR218 4.4 99.1 1.0 CA A:GLY217 4.4 99.7 1.0 N A:THR218 4.4 105.3 1.0 ND1 A:HIS180 4.4 95.9 1.0 CE1 A:HIS180 4.5 96.1 1.0 CA A:VAL244 4.5 99.6 1.0 N A:ARG222 4.6 96.9 1.0 OD2 A:ASP243 4.6 103.3 1.0 CA A:THR218 4.7 101.3 1.0 N A:PHE245 4.7 97.5 1.0 CB A:ASP223 4.7 98.5 1.0 C A:ASP243 4.8 103.9 1.0 CA A:PHE245 4.8 96.7 1.0 CA A:ASP223 4.8 98.1 1.0 N A:VAL220 4.8 96.5 1.0 N A:ASN221 4.9 91.5 1.0 C A:VAL220 4.9 89.9 1.0 CA A:ASP243 4.9 101.2 1.0 OD1 A:ASP219 5.0 92.6 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila


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 Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila within 5.0Å range: probe atom residue distance (Å) B Occ C:K502 b:113.2 occ:1.00 OD1 C:ASP223 2.6 116.3 1.0 O C:GLY217 2.9 105.8 1.0 O C:VAL244 3.0 114.5 1.0 O C:ASP219 3.1 105.6 1.0 O C:ASN221 3.1 106.1 1.0 CG C:ASP223 3.3 111.5 1.0 C C:GLY217 3.4 106.6 1.0 OD2 C:ASP223 3.5 104.0 1.0 OD1 C:ASP243 3.6 119.9 1.0 N C:ASP219 3.6 105.0 1.0 CB C:ASP219 3.7 106.9 1.0 N C:THR218 3.8 111.8 1.0 C C:ASP219 3.8 105.0 1.0 CA C:ASP219 3.9 104.2 1.0 C C:THR218 4.0 105.6 1.0 C C:VAL244 4.1 112.4 1.0 CA C:THR218 4.1 108.0 1.0 CA C:GLY217 4.2 108.0 1.0 C C:ASN221 4.2 109.1 1.0 N C:ASP223 4.3 112.2 1.0 N C:VAL244 4.3 115.8 1.0 ND1 C:HIS180 4.3 106.0 1.0 CG C:ASP243 4.3 114.0 1.0 CE1 C:HIS180 4.4 111.3 1.0 C C:ARG222 4.5 111.8 1.0 CA C:ARG222 4.6 112.9 1.0 CB C:ASP223 4.7 116.7 1.0 CB C:PHE245 4.7 116.2 1.0 OD2 C:ASP243 4.7 114.3 1.0 O C:THR218 4.7 108.3 1.0 CA C:VAL244 4.8 111.4 1.0 O C:PRO328 4.9 107.8 1.0 N C:ARG222 4.9 107.5 1.0 CG C:ASP219 4.9 106.0 1.0 CA C:ASP223 5.0 116.1 1.0

L.G.Graf, C.Moreno-Yruela, C.Qin, S.Schulze, G.J.Palm, O.Schmoeker, N.Wang, D.Hocking, L.Jebeli, B.Girbardt, L.Berndt, D.M.Weis, M.Janetzky, D.Zuehlke, S.Sievers, R.A.Strugnell, C.A.Olsen, K.Hofmann, M.Lammers. Distribution and Diversity of Classical Deacylases in Bacteria Nature Communications 2024.