Sodium in PDB 4gwe: W116L-OYE1 Complexed with (R)-Carvone

All present enzymatic activity of W116L-OYE1 Complexed with (R)-Carvone:
1.6.99.1;

The structure of W116L-OYE1 Complexed with (R)-Carvone, PDB code: 4gwe was solved by Y.A.Pompeu, J.D.Stewart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.16 / 1.45
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	140.780, 140.780, 42.760, 90.00, 90.00, 90.00
R / Rfree (%)	11.5 / 14.5

The structure of W116L-OYE1 Complexed with (R)-Carvone also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Chlorine	(Cl)	1 atom

The binding sites of Sodium atom in the W116L-OYE1 Complexed with (R)-Carvone (pdb code 4gwe). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the W116L-OYE1 Complexed with (R)-Carvone, PDB code: 4gwe:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the W116L-OYE1 Complexed with (R)-Carvone


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of W116L-OYE1 Complexed with (R)-Carvone within 5.0Å range: probe atom residue distance (Å) B Occ A:Na405 b:34.6 occ:1.00 O A:HOH671 2.7 16.5 1.0 OH4 A:1PE406 2.9 32.2 1.0 O A:HOH972 3.2 29.9 1.0 OH5 A:1PE406 3.2 32.2 1.0 CH2 A:TRP396 3.5 21.0 1.0 C14 A:1PE406 3.7 31.3 1.0 C24 A:1PE406 3.7 31.6 1.0 C25 A:1PE406 3.8 34.0 1.0 C15 A:1PE406 3.8 36.8 1.0 N A:SER1 3.9 18.0 1.0 CZ2 A:TRP396 4.0 20.9 1.0 OH6 A:1PE406 4.0 38.2 1.0 C26 A:1PE406 4.3 37.8 1.0 O A:LYS368 4.4 14.2 1.0 CE1 A:TYR385 4.4 10.7 1.0 CZ3 A:TRP396 4.4 21.0 1.0 CD1 A:TYR385 4.5 11.2 1.0 O A:HOH956 4.8 36.3 1.0 O A:HOH998 5.0 42.8 1.0

Sodium binding site 2 out of 2 in the W116L-OYE1 Complexed with (R)-Carvone


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of W116L-OYE1 Complexed with (R)-Carvone within 5.0Å range: probe atom residue distance (Å) B Occ A:Na408 b:38.0 occ:1.00 O A:HOH901 2.2 81.0 1.0 OH5 A:1PE404 2.8 29.7 0.9 NE1 A:TRP52 3.0 12.7 1.0 OH6 A:1PE404 3.0 30.1 0.9 OH4 A:1PE404 3.1 32.4 0.9 C24 A:1PE404 3.4 30.6 0.9 O A:HOH1054 3.4 42.2 1.0 C14 A:1PE404 3.6 29.6 0.9 C13 A:1PE404 3.7 32.0 0.9 C26 A:1PE404 3.7 29.9 0.9 C16 A:1PE404 3.7 31.4 0.9 CD1 A:TRP52 3.8 12.6 1.0 C15 A:1PE404 3.8 29.1 0.9 C25 A:1PE404 3.8 29.3 0.9 CE2 A:TRP52 4.0 13.1 1.0 O A:HOH1040 4.3 38.3 1.0 CZ2 A:TRP52 4.5 12.8 1.0 CB A:ASP51 4.6 13.1 1.0

Y.A.Pompeu, B.Sullivan, J.D.Stewart. X‑Ray Crystallography Reveals How Subtle Changes Control the Orientation of Substrate Binding in An Alkene Reductase Acs Catalysis V. 3 2376 2013.
ISSN: ESSN 2155-5435
DOI: 10.1021/CS400622E