Potassium in PDB 9phg: Ketoreductase Engineering For A Chemoenzymatic Fluorination and Dynamic Kinetic Reduction Cascade

All present enzymatic activity of Ketoreductase Engineering For A Chemoenzymatic Fluorination and Dynamic Kinetic Reduction Cascade:
1.1.1.2;

The structure of Ketoreductase Engineering For A Chemoenzymatic Fluorination and Dynamic Kinetic Reduction Cascade, PDB code: 9phg was solved by A.Hruza, S.Chun, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.88 / 1.48
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	44.599, 52.463, 83.861, 75.95, 84.06, 66.05
R / Rfree (%)	17.4 / 19.5

The binding sites of Potassium atom in the Ketoreductase Engineering For A Chemoenzymatic Fluorination and Dynamic Kinetic Reduction Cascade (pdb code 9phg). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Ketoreductase Engineering For A Chemoenzymatic Fluorination and Dynamic Kinetic Reduction Cascade, PDB code: 9phg:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Ketoreductase Engineering For A Chemoenzymatic Fluorination and Dynamic Kinetic Reduction Cascade


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Ketoreductase Engineering For A Chemoenzymatic Fluorination and Dynamic Kinetic Reduction Cascade within 5.0Å range: probe atom residue distance (Å) B Occ A:K402 b:23.3 occ:1.00 HE21 A:GLN31 2.2 20.7 0.0 HZ A:PHE214 2.9 19.4 0.0 HA A:PHE251 2.9 12.2 0.0 HD1 A:PHE251 3.0 15.9 0.0 ND1 A:HIS27 3.1 15.6 1.0 HG2 A:GLN31 3.1 17.5 0.0 HG2 A:GLU30 3.1 17.3 0.0 NE2 A:GLN31 3.2 20.0 1.0 O A:HOH688 3.3 31.7 1.0 HB3 A:GLU30 3.4 16.5 0.0 HB3 A:HIS27 3.6 11.6 0.0 HA A:HIS27 3.6 11.9 0.0 HB2 A:PHE251 3.8 12.9 0.0 HE22 A:GLN31 3.8 21.1 0.0 CA A:PHE251 3.9 12.3 1.0 CZ A:PHE214 3.9 18.6 1.0 CG A:GLN31 3.9 17.2 1.0 CE1 A:HIS27 4.0 15.3 1.0 CD1 A:PHE251 4.0 15.4 1.0 CD A:GLN31 4.0 18.7 1.0 CG A:HIS27 4.1 13.2 1.0 HE1 A:HIS27 4.1 15.5 0.0 CG A:GLU30 4.1 16.2 1.0 O A:HIS27 4.2 13.8 1.0 CB A:HIS27 4.2 12.0 1.0 CB A:GLU30 4.2 15.8 1.0 O A:HOH588 4.2 41.5 1.0 HG3 A:GLN31 4.2 17.4 0.0 CB A:PHE251 4.3 12.8 1.0 CA A:HIS27 4.3 11.8 1.0 HE2 A:PHE214 4.3 19.9 0.0 HG3 A:GLU30 4.5 17.6 0.0 HA3 A:GLY254 4.5 11.4 0.0 N A:PHE251 4.6 11.4 1.0 CE2 A:PHE214 4.6 19.3 1.0 CG A:PHE251 4.6 13.8 1.0 H A:GLN31 4.6 13.8 0.0 HB2 A:GLU30 4.7 16.8 0.0 C A:HIS27 4.7 12.7 1.0 O A:ALA250 4.7 13.5 1.0 HE1 A:PHE214 4.8 20.5 0.0 O A:PHE251 4.8 12.9 1.0 CE1 A:PHE214 4.8 19.3 1.0 C A:PHE251 4.9 12.0 1.0 C A:ALA250 4.9 12.3 1.0 N A:GLN31 5.0 13.3 1.0 HE1 A:PHE251 5.0 17.6 0.0 CE1 A:PHE251 5.0 16.6 1.0

Potassium binding site 2 out of 2 in the Ketoreductase Engineering For A Chemoenzymatic Fluorination and Dynamic Kinetic Reduction Cascade


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Ketoreductase Engineering For A Chemoenzymatic Fluorination and Dynamic Kinetic Reduction Cascade within 5.0Å range: probe atom residue distance (Å) B Occ B:K402 b:23.0 occ:1.00 HE21 B:GLN31 2.2 19.9 0.0 HA B:PHE251 2.9 13.4 0.0 HD1 B:PHE251 2.9 17.3 0.0 HZ B:PHE214 2.9 19.8 0.0 HG2 B:GLU30 3.0 15.8 0.0 ND1 B:HIS27 3.1 16.8 1.0 O B:HOH663 3.1 26.1 1.0 NE2 B:GLN31 3.2 19.6 1.0 HG2 B:GLN31 3.2 15.2 0.0 HB3 B:GLU30 3.3 16.4 0.0 HA B:HIS27 3.6 11.5 0.0 HB2 B:PHE251 3.7 14.0 0.0 HB3 B:HIS27 3.7 12.2 0.0 HE22 B:GLN31 3.7 20.3 0.0 CA B:PHE251 3.9 13.8 1.0 CD1 B:PHE251 3.9 17.0 1.0 CG B:GLU30 3.9 15.3 1.0 CE1 B:HIS27 3.9 16.6 1.0 O B:HOH564 4.0 37.8 1.0 CZ B:PHE214 4.0 19.6 1.0 CG B:GLN31 4.0 15.3 1.0 HE1 B:HIS27 4.0 16.4 0.0 CD B:GLN31 4.0 19.1 1.0 CG B:HIS27 4.1 13.6 1.0 CB B:GLU30 4.1 16.3 1.0 O B:HIS27 4.1 13.1 1.0 CB B:PHE251 4.2 13.9 1.0 CB B:HIS27 4.2 12.9 1.0 HG3 B:GLU30 4.3 16.1 0.0 CA B:HIS27 4.3 11.9 1.0 HE2 B:PHE214 4.4 19.8 0.0 HG3 B:GLN31 4.4 15.2 0.0 CG B:PHE251 4.5 15.1 1.0 HB2 B:GLU30 4.5 16.6 0.0 N B:PHE251 4.5 12.9 1.0 HA3 B:GLY254 4.6 11.0 0.0 CE2 B:PHE214 4.6 19.8 1.0 C B:HIS27 4.7 12.2 1.0 H B:GLN31 4.8 13.6 0.0 O B:ALA250 4.8 13.2 1.0 O B:PHE251 4.9 13.9 1.0 HE1 B:PHE251 4.9 18.7 0.0 HE1 B:PHE214 4.9 20.0 0.0 CE1 B:PHE251 4.9 17.8 1.0 C B:PHE251 4.9 13.3 1.0 CE1 B:PHE214 4.9 19.3 1.0 C B:ALA250 5.0 13.3 1.0 O B:HOH647 5.0 31.6 1.0

S.W.Chun, B.Kosjek, J.K.B.Cahn, A.M.Makarewicz, W.L.Cheung-Lee, D.Verma, C.M.Jones, A.Hruza, J.H.Forstater, S.Li, Q.Gallagher, G.S.Murphy, J.C.Moore. Ketoreductase Engineering For A Chemoenzymatic Fluorination and Dynamic Kinetic Reduction Cascade Acs Catalysis 13059 2025.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.5C01769