Potassium in PDB 5ohs: A GH31 Family Sulfoquinovosidase Mutant D455N in Complex with Pnpsq

All present enzymatic activity of A GH31 Family Sulfoquinovosidase Mutant D455N in Complex with Pnpsq:
3.2.1.20;

The structure of A GH31 Family Sulfoquinovosidase Mutant D455N in Complex with Pnpsq, PDB code: 5ohs was solved by Y.Jin, S.J.Williams, E.Goddard-Borger, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	75.77 / 1.97
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	104.200, 169.190, 169.690, 90.00, 92.80, 90.00
R / Rfree (%)	18.1 / 20.3

The structure of A GH31 Family Sulfoquinovosidase Mutant D455N in Complex with Pnpsq also contains other interesting chemical elements:

Chlorine

(Cl)

6 atoms

The binding sites of Potassium atom in the A GH31 Family Sulfoquinovosidase Mutant D455N in Complex with Pnpsq (pdb code 5ohs). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the A GH31 Family Sulfoquinovosidase Mutant D455N in Complex with Pnpsq, PDB code: 5ohs:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the A GH31 Family Sulfoquinovosidase Mutant D455N in Complex with Pnpsq


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of A GH31 Family Sulfoquinovosidase Mutant D455N in Complex with Pnpsq within 5.0Å range: probe atom residue distance (Å) B Occ C:K701 b:37.7 occ:1.00 OH C:TYR319 2.9 39.6 1.0 N C:GLY390 3.1 24.5 1.0 N C:TYR392 3.3 27.1 1.0 CZ C:TYR319 3.3 35.9 1.0 C C:GLY390 3.4 25.4 1.0 CA C:GLY390 3.4 24.9 1.0 CE2 C:TYR319 3.6 34.3 1.0 N C:LEU393 3.6 28.9 1.0 C C:TYR392 3.6 29.9 1.0 N C:GLU391 3.7 25.6 1.0 CB C:TYR392 3.8 33.1 1.0 O C:GLY390 3.8 27.4 1.0 CA C:TYR392 3.8 29.3 1.0 CD1 C:TRP412 4.0 30.5 1.0 CB C:PHE389 4.1 23.1 1.0 O C:TYR392 4.3 38.0 1.0 C C:PHE389 4.3 24.4 1.0 C C:GLU391 4.4 28.4 1.0 CG C:PRO318 4.4 26.8 1.0 CA C:LEU393 4.5 29.2 1.0 CE1 C:TYR319 4.5 32.9 1.0 CA C:GLU391 4.5 26.6 1.0 NE1 C:TRP412 4.5 31.4 1.0 CA C:PHE389 4.7 23.6 1.0 O C:HOH863 4.7 20.6 1.0 CD2 C:TYR319 4.8 32.1 1.0 CB C:LEU393 4.9 30.8 1.0 CD2 C:PHE389 4.9 21.5 1.0 OE1 C:GLU391 5.0 26.0 1.0 CG C:TRP412 5.0 30.2 1.0

Potassium binding site 2 out of 2 in the A GH31 Family Sulfoquinovosidase Mutant D455N in Complex with Pnpsq


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of A GH31 Family Sulfoquinovosidase Mutant D455N in Complex with Pnpsq within 5.0Å range: probe atom residue distance (Å) B Occ D:K701 b:33.5 occ:1.00 OH D:TYR319 2.9 36.6 1.0 N D:GLY390 3.1 21.3 1.0 N D:TYR392 3.3 24.9 1.0 CZ D:TYR319 3.4 30.4 1.0 C D:GLY390 3.4 22.5 1.0 CA D:GLY390 3.4 21.9 1.0 CE2 D:TYR319 3.6 30.7 1.0 N D:GLU391 3.6 23.0 1.0 N D:LEU393 3.7 27.1 1.0 C D:TYR392 3.7 27.2 1.0 O D:GLY390 3.8 23.4 1.0 CB D:TYR392 3.8 29.4 1.0 CA D:TYR392 3.8 27.0 1.0 CD1 D:TRP412 4.0 28.5 1.0 CB D:PHE389 4.1 20.3 1.0 C D:PHE389 4.3 20.4 1.0 O D:TYR392 4.3 32.3 1.0 C D:GLU391 4.4 24.9 1.0 CG D:PRO318 4.4 24.7 1.0 CA D:LEU393 4.5 26.8 1.0 CE1 D:TYR319 4.5 29.4 1.0 NE1 D:TRP412 4.5 30.5 1.0 CA D:GLU391 4.5 23.3 1.0 CA D:PHE389 4.7 19.9 1.0 CD2 D:TYR319 4.8 29.1 1.0 O D:HOH890 4.8 18.7 1.0 CD2 D:PHE389 4.9 20.0 1.0 CB D:LEU393 4.9 27.4 1.0 OE1 D:GLU391 4.9 22.4 1.0 CG D:TRP412 5.0 27.5 1.0 CG D:PHE389 5.0 20.1 1.0

P.Abayakoon, Y.Jin, J.P.Lingford, M.Petricevic, A.John, E.Ryan, J.Wai-Ying Mui, D.E.V.Pires, D.B.Ascher, G.J.Davies, E.D.Goddard-Borger, S.J.Williams. Structural and Biochemical Insights Into the Function and Evolution of Sulfoquinovosidases. Acs Cent Sci V. 4 1266 2018.
ISSN: ESSN 2374-7943
PubMed: 30276262
DOI: 10.1021/ACSCENTSCI.8B00453