Potassium in PDB 6p9v: Crystal Structure of Hmat Mutant K289L

All present enzymatic activity of Crystal Structure of Hmat Mutant K289L:
2.5.1.6;

The structure of Crystal Structure of Hmat Mutant K289L, PDB code: 6p9v was solved by M.D.Miller, W.Xu, T.D.Huber, J.A.Clinger, Y.Liu, J.S.Thorson, G.N.Philipsjr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.74 / 2.05
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	66.348, 94.624, 116.573, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 20.3

The structure of Crystal Structure of Hmat Mutant K289L also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Potassium atom in the Crystal Structure of Hmat Mutant K289L (pdb code 6p9v). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Crystal Structure of Hmat Mutant K289L, PDB code: 6p9v:

Potassium binding site 1 out of 1 in the Crystal Structure of Hmat Mutant K289L


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 Hmat Mutant K289L within 5.0Å range: probe atom residue distance (Å) B Occ A:K402 b:39.5 occ:1.00 O4 A:POP404 2.7 7.1 0.2 O2 A:POP404 2.7 7.1 0.2 OD1 A:ASP258 2.8 52.4 1.0 O A:HOH625 2.9 8.4 0.5 O A:HOH634 3.0 14.6 0.5 O A:HOH508 3.0 13.5 1.0 O A:ALA259 3.1 27.7 1.0 O A:HOH545 3.1 21.4 1.0 OD2 A:ASP258 3.4 50.1 1.0 CG A:ASP258 3.4 50.5 1.0 MG A:MG403 3.7 13.8 1.0 O5 A:POP404 3.7 6.9 0.2 P2 A:POP404 3.7 7.6 0.2 HB3 A:ALA259 3.8 34.1 1.0 HH22 A:ARG264 4.0 37.5 1.0 P1 A:POP404 4.1 7.2 0.2 H A:ALA259 4.1 41.7 1.0 C A:ALA259 4.1 25.9 1.0 N A:ALA259 4.3 34.7 1.0 O A:POP404 4.4 8.4 0.2 NH2 A:ARG264 4.4 31.2 1.0 O6 A:POP404 4.6 8.5 0.2 CA A:ALA259 4.6 27.6 1.0 CB A:ALA259 4.6 28.4 1.0 O1 A:POP404 4.6 7.7 0.2 HH21 A:ARG264 4.6 37.5 1.0 O3 A:POP404 4.6 8.8 0.2 O A:HOH502 4.7 10.4 0.3 O4 A:POP404 4.8 10.2 0.2 CB A:ASP258 4.8 48.3 1.0 C A:ASP258 4.8 40.1 1.0 O A:HOH501 4.8 9.9 0.5 O5 A:POP404 4.9 11.1 0.2 H5'1 A:ADN401 4.9 42.2 1.0 HA A:ASP258 4.9 55.7 1.0 HA2 A:GLY260 5.0 32.7 1.0

T.D.Huber, J.A.Clinger, Y.Liu, W.Xu, M.D.Miller, G.N.Phillips Jr., J.S.Thorson. Methionine Adenosyltransferase Engineering to Enable Bioorthogonal Platforms For Adomet-Utilizing Enzymes. Acs Chem.Biol. V. 15 695 2020.
ISSN: ESSN 1554-8937
PubMed: 32091873
DOI: 10.1021/ACSCHEMBIO.9B00943