Potassium in PDB 1lqp: Crystal Structure of the Fosfomycin Resistance Protein (Fosa) Containing Bound Substrate

All present enzymatic activity of Crystal Structure of the Fosfomycin Resistance Protein (Fosa) Containing Bound Substrate:
2.5.1.18;

The structure of Crystal Structure of the Fosfomycin Resistance Protein (Fosa) Containing Bound Substrate, PDB code: 1lqp was solved by C.L.Rife, R.E.Pharris, M.E.Newcomer, R.N.Armstrong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.19
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.071, 64.901, 76.730, 90.00, 90.00, 90.00
R / Rfree (%)	15.6 / 20

The structure of Crystal Structure of the Fosfomycin Resistance Protein (Fosa) Containing Bound Substrate also contains other interesting chemical elements:

Manganese

(Mn)

2 atoms

The binding sites of Potassium atom in the Crystal Structure of the Fosfomycin Resistance Protein (Fosa) Containing Bound Substrate (pdb code 1lqp). 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 Fosfomycin Resistance Protein (Fosa) Containing Bound Substrate, PDB code: 1lqp:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of the Fosfomycin Resistance Protein (Fosa) Containing Bound Substrate


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 Fosfomycin Resistance Protein (Fosa) Containing Bound Substrate within 5.0Å range: probe atom residue distance (Å) B Occ A:K3002 b:14.6 occ:1.00 OD1 A:ASN92 2.6 15.8 1.0 OG A:SER94 2.7 15.6 1.0 O A:GLY96 2.7 16.2 1.0 OG A:SER98 2.8 13.8 1.0 O A:HOH9016 2.9 14.9 1.0 O A:SER94 2.9 16.1 1.0 O A:GLU95 2.9 15.9 1.0 C A:SER94 3.4 15.1 1.0 CG A:ASN92 3.5 15.7 1.0 CB A:SER98 3.6 12.8 1.0 CE1 A:HIS112 3.6 14.5 1.0 C A:GLU95 3.6 15.0 1.0 NH2 A:ARG119 3.7 15.4 1.0 ND1 A:HIS112 3.7 13.9 1.0 ND2 A:ASN92 3.8 20.6 1.0 CB A:SER94 3.8 16.0 1.0 C A:GLY96 3.8 15.8 1.0 OH A:TYR100 3.9 13.9 1.0 CA A:SER94 3.9 15.8 1.0 N A:SER94 4.1 15.8 1.0 N A:GLU95 4.1 15.2 1.0 N A:GLY96 4.3 16.0 1.0 O3P A:FCN4002 4.4 14.5 1.0 N A:SER98 4.4 13.4 1.0 O A:HOH9013 4.4 16.1 1.0 CA A:GLY96 4.4 15.7 1.0 C A:ASP97 4.5 14.2 1.0 CA A:GLU95 4.5 15.1 1.0 OE2 A:GLU110 4.5 13.0 1.0 O A:ASP97 4.6 14.4 1.0 CA A:SER98 4.6 13.3 1.0 NE2 A:HIS112 4.7 14.2 1.0 CZ A:ARG119 4.9 14.5 1.0 CB A:ASN92 4.9 14.7 1.0 N A:ASP97 4.9 15.8 1.0 CG A:HIS112 4.9 13.4 1.0 CZ A:TYR100 5.0 13.3 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of the Fosfomycin Resistance Protein (Fosa) Containing Bound Substrate


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 Fosfomycin Resistance Protein (Fosa) Containing Bound Substrate within 5.0Å range: probe atom residue distance (Å) B Occ B:K3001 b:16.5 occ:1.00 OD1 B:ASN92 2.6 18.8 1.0 O B:GLY96 2.7 19.3 1.0 OG B:SER94 2.7 17.1 1.0 O B:HOH9014 2.8 15.7 1.0 OG B:SER98 2.8 15.6 1.0 O B:GLU95 2.9 17.4 1.0 O B:SER94 3.0 18.8 1.0 C B:SER94 3.4 17.8 1.0 CG B:ASN92 3.5 17.5 1.0 CB B:SER98 3.5 15.0 1.0 CE1 B:HIS112 3.6 16.1 1.0 C B:GLU95 3.7 17.2 1.0 NH2 B:ARG119 3.7 18.4 1.0 ND2 B:ASN92 3.7 22.4 1.0 ND1 B:HIS112 3.8 15.7 1.0 C B:GLY96 3.8 17.6 1.0 CB B:SER94 3.8 18.0 1.0 OH B:TYR100 3.9 15.8 1.0 CA B:SER94 3.9 18.6 1.0 N B:SER94 4.1 18.4 1.0 N B:GLU95 4.2 17.9 1.0 N B:GLY96 4.3 19.1 1.0 CA B:GLY96 4.4 19.1 1.0 O3P B:FCN4001 4.4 16.4 1.0 N B:SER98 4.4 15.5 1.0 O B:HOH9076 4.4 18.6 1.0 C B:ASP97 4.5 16.2 1.0 OE2 B:GLU110 4.5 14.9 1.0 CA B:GLU95 4.6 18.6 1.0 CA B:SER98 4.6 15.2 1.0 O B:ASP97 4.6 16.4 1.0 NE2 B:HIS112 4.7 15.9 1.0 CB B:ASN92 4.8 16.9 1.0 N B:ASP97 4.9 17.8 1.0 CZ B:ARG119 4.9 17.7 1.0 CZ B:TYR100 4.9 14.2 1.0 CG B:HIS112 4.9 15.1 1.0

C.L.Rife, R.E.Pharris, M.E.Newcomer, R.N.Armstrong. Crystal Structure of A Genomically Encoded Fosfomycin Resistance Protein (Fosa) at 1.19 A Resolution By Mad Phasing Off the L-III Edge of Tl(+) J.Am.Chem.Soc. V. 124 11001 2002.
ISSN: ISSN 0002-7863
PubMed: 12224946
DOI: 10.1021/JA026879V