Potassium in PDB 4n3d: Crystal Structure of the Dimeric Variant Egfp-K162Q in P61 Space Group

The structure of Crystal Structure of the Dimeric Variant Egfp-K162Q in P61 Space Group, PDB code: 4n3d was solved by N.V.Pletneva, V.Z.Pletnev, S.V.Pletnev, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.21 / 1.34
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	121.861, 121.861, 64.891, 90.00, 90.00, 120.00
R / Rfree (%)	18.1 / 19.4

The binding sites of Potassium atom in the Crystal Structure of the Dimeric Variant Egfp-K162Q in P61 Space Group (pdb code 4n3d). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the Crystal Structure of the Dimeric Variant Egfp-K162Q in P61 Space Group, PDB code: 4n3d:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in the Crystal Structure of the Dimeric Variant Egfp-K162Q in P61 Space Group


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 the Dimeric Variant Egfp-K162Q in P61 Space Group within 5.0Å range: probe atom residue distance (Å) B Occ A:K303 b:20.5 occ:0.60 OE2 A:GLU172 2.7 24.8 0.7 O A:HIS139 2.7 13.6 1.0 O A:HOH668 2.7 38.0 1.0 O A:HOH516 3.0 29.9 1.0 O A:HOH427 3.1 15.5 1.0 O A:HOH521 3.1 25.5 1.0 O A:HOH590 3.2 32.5 1.0 O A:HOH488 3.2 23.2 1.0 CD A:GLU172 3.6 20.2 0.6 C A:HIS139 3.7 12.5 1.0 O A:LEU141 3.8 16.1 1.0 OE1 A:GLU172 3.9 22.9 0.7 O A:HOH421 4.2 14.0 1.0 K A:K305 4.2 9.6 0.6 CB A:HIS139 4.2 13.6 1.0 N A:LYS140 4.5 13.2 1.0 CA A:HIS139 4.5 12.8 1.0 CA A:LYS140 4.6 14.3 1.0 N A:LEU141 4.6 12.9 1.0 CG A:GLU172 4.8 17.7 0.6 C A:LYS140 4.8 13.9 1.0 C A:LEU141 4.8 12.9 1.0 O A:HOH425 4.9 16.7 1.0

Potassium binding site 2 out of 3 in the Crystal Structure of the Dimeric Variant Egfp-K162Q in P61 Space Group


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of the Dimeric Variant Egfp-K162Q in P61 Space Group within 5.0Å range: probe atom residue distance (Å) B Occ A:K304 b:14.7 occ:0.90 O A:HOH432 2.7 14.1 1.0 O B:HOH317 2.7 14.2 1.0 O A:SER205 2.8 13.0 1.0 O B:SER205 2.9 13.5 1.0 O A:TYR145 2.9 11.9 1.0 O B:HOH319 3.0 15.3 1.0 O A:HOH448 3.2 20.0 1.0 O A:HOH418 3.6 13.3 1.0 O B:TYR145 3.7 11.8 1.0 C B:SER205 4.0 11.5 1.0 C A:SER205 4.1 12.5 1.0 C A:TYR145 4.1 10.2 1.0 N B:SER205 4.3 13.2 1.0 N A:SER205 4.4 12.8 1.0 O B:HOH349 4.5 18.7 1.0 O A:HOH546 4.6 28.2 1.0 OG B:SER147 4.7 12.8 1.0 OG A:SER147 4.7 12.2 1.0 CA B:SER205 4.8 14.0 1.0 CA A:SER205 4.9 12.3 1.0 N A:TYR145 4.9 10.3 1.0 CB B:GLN204 4.9 16.6 1.0 N B:ALA206 4.9 12.7 1.0 N A:ALA206 4.9 11.4 1.0 CA A:TYR145 5.0 10.6 1.0 CA A:ASN146 5.0 10.2 1.0 O A:ASN146 5.0 11.6 1.0 CA A:ALA206 5.0 12.3 1.0 N A:ASN146 5.0 10.0 1.0 C B:TYR145 5.0 11.6 1.0 C A:ASN146 5.0 10.7 1.0

Potassium binding site 3 out of 3 in the Crystal Structure of the Dimeric Variant Egfp-K162Q in P61 Space Group


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Crystal Structure of the Dimeric Variant Egfp-K162Q in P61 Space Group within 5.0Å range: probe atom residue distance (Å) B Occ A:K305 b:9.6 occ:0.60 O A:HIS139 2.8 13.6 1.0 O A:HOH521 2.8 25.5 1.0 O A:HOH632 2.8 30.5 1.0 O A:GLY138 2.9 14.8 1.0 O A:HOH502 2.9 20.4 1.0 O A:HOH590 3.0 32.5 1.0 C A:HIS139 3.5 12.5 1.0 CB A:HIS139 3.7 13.6 1.0 O A:HOH549 3.9 28.7 1.0 C A:GLY138 4.0 14.0 1.0 CA A:HIS139 4.1 12.8 1.0 K A:K303 4.2 20.5 0.6 N A:LYS140 4.5 13.2 1.0 N A:HIS139 4.6 13.3 1.0 CG A:LYS140 4.8 17.5 1.0 OE1 A:GLU172 4.8 22.9 0.7 CA A:LYS140 4.8 14.3 1.0 O A:HOH526 4.8 24.7 1.0 CG A:HIS139 5.0 12.7 1.0

N.V.Pletneva, S.V Pletnev, A.M.Bogdanov, E.A.Goryacheva, I.V.Artemyev, E.A.Souslova, S.F.Arkhipova, V.Z.Pletnev. Three Dimensional Structure of the Dimeric Gene-Engineered Variant of Green Fluorescent Protein Egfp-K162Q in P61 Crystal Space Group Rus.J.Bioorg.Chem. V. 40 383 2014.