Potassium in PDB 5kmt: Ctx-M9 Mutant L48A

All present enzymatic activity of Ctx-M9 Mutant L48A:
3.5.2.6;

The structure of Ctx-M9 Mutant L48A, PDB code: 5kmt was solved by M.J.Latallo, S.Faham, P.M.Kasson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.22 / 1.70
Space group	P 32
Cell size a, b, c (Å), α, β, γ (°)	41.788, 41.788, 232.401, 90.00, 90.00, 120.00
R / Rfree (%)	19.4 / 21.6

The binding sites of Potassium atom in the Ctx-M9 Mutant L48A (pdb code 5kmt). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the Ctx-M9 Mutant L48A, PDB code: 5kmt:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in the Ctx-M9 Mutant L48A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Ctx-M9 Mutant L48A within 5.0Å range: probe atom residue distance (Å) B Occ A:K303 b:21.7 occ:1.00 O A:HOH550 2.7 36.4 1.0 O A:SER130 2.7 14.0 1.0 O A:HOH533 2.8 15.9 1.0 O4 A:PO4302 2.8 18.4 1.0 OG A:SER70 2.9 11.0 1.0 OG A:SER130 2.9 12.9 1.0 OD1 A:ASN132 3.0 12.4 1.0 CB A:SER130 3.5 13.9 1.0 CG A:ASN132 3.8 12.8 1.0 O A:HOH483 3.8 11.7 1.0 C A:SER130 3.8 14.4 1.0 ND2 A:ASN132 3.8 13.1 1.0 CD2 A:TYR105 4.0 27.6 1.0 O A:HOH412 4.0 16.0 1.0 CB A:SER70 4.0 10.7 1.0 P A:PO4302 4.1 20.1 1.0 CA A:SER130 4.2 14.3 1.0 NZ A:LYS73 4.2 10.9 1.0 O3 A:PO4302 4.4 20.7 1.0 O2 A:PO4302 4.4 21.9 1.0 CE A:LYS73 4.5 11.5 1.0 CE2 A:TYR105 4.5 28.6 1.0 CG A:TYR105 4.9 27.6 1.0 N A:ASP131 4.9 15.0 1.0 N A:ASN132 5.0 14.0 1.0 CB A:TYR105 5.0 26.0 1.0

Potassium binding site 2 out of 4 in the Ctx-M9 Mutant L48A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Ctx-M9 Mutant L48A within 5.0Å range: probe atom residue distance (Å) B Occ A:K304 b:52.6 occ:1.00 O A:HOH543 3.0 33.7 1.0 OG A:SER272 3.7 19.0 1.0 CB A:SER272 4.1 18.4 1.0 O A:HOH534 4.6 25.4 1.0 O A:HOH461 4.7 34.5 1.0 O A:HOH536 4.8 28.0 1.0

Potassium binding site 3 out of 4 in the Ctx-M9 Mutant L48A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Ctx-M9 Mutant L48A within 5.0Å range: probe atom residue distance (Å) B Occ A:K305 b:33.9 occ:1.00 OD1 A:ASN214 2.5 17.6 1.0 OG1 A:THR216 2.7 15.9 1.0 O A:LEU127 2.8 16.2 1.0 NZ A:LYS234 3.0 13.6 1.0 CG A:ASN214 3.2 17.7 1.0 CE A:LYS234 3.4 13.7 1.0 ND2 A:ASN214 3.5 16.9 1.0 CD A:LYS234 3.5 13.9 1.0 CG2 A:THR216 3.7 17.3 1.0 CB A:THR216 3.8 16.7 1.0 C A:LEU127 3.8 16.5 1.0 OG1 A:THR235 3.8 13.2 1.0 N A:SER130 4.0 15.5 1.0 CB A:SER130 4.1 13.9 1.0 C A:GLN128 4.1 18.3 1.0 N A:THR235 4.1 12.8 1.0 O A:GLN128 4.2 18.6 1.0 CA A:GLN128 4.4 18.6 1.0 O A:HOH465 4.4 21.0 1.0 N A:TYR129 4.4 17.8 1.0 CA A:SER130 4.5 14.3 1.0 N A:GLN128 4.5 17.7 1.0 CB A:ASN214 4.5 18.8 1.0 CA A:LYS234 4.5 13.9 1.0 OG A:SER130 4.5 12.9 1.0 CG A:LYS234 4.6 13.2 1.0 N A:THR216 4.6 18.6 1.0 C A:TYR129 4.6 16.5 1.0 O A:ALA126 4.7 14.4 1.0 CA A:THR216 4.8 17.6 1.0 CA A:LEU127 4.8 15.8 1.0 CB A:THR235 4.9 12.7 1.0 CA A:TYR129 4.9 17.8 1.0 C A:LYS234 4.9 13.0 1.0 O A:ASP233 4.9 16.3 1.0 O A:THR235 5.0 11.6 1.0 CA A:THR235 5.0 12.2 1.0

Potassium binding site 4 out of 4 in the Ctx-M9 Mutant L48A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Ctx-M9 Mutant L48A within 5.0Å range: probe atom residue distance (Å) B Occ B:K303 b:29.2 occ:1.00 O B:HOH475 2.6 22.0 1.0 O B:GLY238 2.7 14.4 1.0 O B:HOH529 2.7 28.2 1.0 O B:HOH489 3.0 20.3 1.0 C B:GLY238 3.5 14.4 1.0 O B:ALA270 4.2 20.4 1.0 N B:ASP239 4.2 15.1 1.0 CA B:GLY238 4.2 13.6 1.0 N B:GLY238 4.3 12.9 1.0 CA B:ASP239 4.4 16.1 1.0 CA B:GLY241 4.5 13.0 1.0 OG B:SER272 4.5 18.3 1.0 N B:GLY241 4.6 13.7 1.0 C B:ASP239 4.9 15.2 1.0 N B:THR242 4.9 11.3 1.0 OD1 B:ASP239 5.0 20.0 1.0

M.J.Latallo, G.A.Cortina, S.Faham, R.K.Nakamoto, P.M.Kasson. Predicting Allosteric Mutants That Increase Activity of A Major Antibiotic Resistance Enzyme. Chem Sci V. 8 6484 2017.
ISSN: ISSN 2041-6520
PubMed: 28989673
DOI: 10.1039/C7SC02676E