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Potassium in PDB 8vqk: Ycjn From Escherichia Coli

Protein crystallography data

The structure of Ycjn From Escherichia Coli, PDB code: 8vqk was solved by M.A.Trevino, D.Fernandez, N.G.Sharaf, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.65 / 1.95
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 63.216, 63.29, 74.314, 110.01, 91.09, 118.66
R / Rfree (%) 21.5 / 26.4

Other elements in 8vqk:

The structure of Ycjn From Escherichia Coli also contains other interesting chemical elements:

Cadmium (Cd) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Ycjn From Escherichia Coli (pdb code 8vqk). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the Ycjn From Escherichia Coli, PDB code: 8vqk:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 8vqk

Go back to Potassium Binding Sites List in 8vqk
Potassium binding site 1 out of 4 in the Ycjn From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Ycjn From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K504

b:35.8
occ:1.00
OE2 A:GLU87 2.2 44.2 1.0
OE1 A:GLU87 2.7 37.1 1.0
CD A:GLU87 2.8 40.8 1.0
OE2 A:GLU32 2.9 52.4 1.0
CD A:GLU32 3.6 49.5 1.0
CG A:GLU32 3.8 45.5 1.0
OE2 A:GLU311 4.2 51.5 1.0
O A:SER30 4.3 38.4 1.0
CG A:GLU87 4.3 36.9 1.0
CD A:GLU311 4.3 46.6 1.0
OE1 A:GLN307 4.4 44.0 1.0
OE1 A:GLU311 4.4 43.6 1.0
O A:HOH672 4.5 47.5 1.0
OE1 A:GLU32 4.5 55.1 1.0
CA A:ILE31 4.6 31.3 1.0
N A:GLU32 4.7 35.3 1.0
O A:LEU85 4.8 37.1 1.0
N A:GLU87 5.0 33.2 1.0
C A:ILE31 5.0 35.8 1.0

Potassium binding site 2 out of 4 in 8vqk

Go back to Potassium Binding Sites List in 8vqk
Potassium binding site 2 out of 4 in the Ycjn From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Ycjn From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K505

b:39.0
occ:1.00
OD2 A:ASP106 2.5 45.2 1.0
O A:HOH744 2.9 54.6 1.0
OD1 A:ASP106 2.9 38.0 1.0
CG A:ASP106 3.0 41.5 1.0
O A:HOH690 4.5 42.0 1.0
CB A:ASP106 4.5 32.5 1.0
O A:HOH622 4.6 36.2 1.0
CG2 A:THR312 4.7 31.4 1.0
CB A:LYS108 4.9 39.6 1.0

Potassium binding site 3 out of 4 in 8vqk

Go back to Potassium Binding Sites List in 8vqk
Potassium binding site 3 out of 4 in the Ycjn From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Ycjn From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K506

b:70.3
occ:1.00
OE1 B:GLU313 2.5 67.1 1.0
OE2 B:GLU313 2.7 78.4 1.0
CD B:GLU313 2.9 66.0 1.0
O B:HOH740 4.1 64.8 1.0
CG B:GLU313 4.4 53.0 1.0
CB B:GLU313 5.0 42.8 1.0

Potassium binding site 4 out of 4 in 8vqk

Go back to Potassium Binding Sites List in 8vqk
Potassium binding site 4 out of 4 in the Ycjn From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Ycjn From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K507

b:35.0
occ:1.00
OE2 B:GLU87 2.3 41.2 1.0
OE1 B:GLU87 2.6 33.6 1.0
CD B:GLU87 2.7 36.9 1.0
OE2 B:GLU311 4.1 55.8 1.0
OE1 B:GLU32 4.2 51.8 1.0
CD B:GLU32 4.2 50.9 1.0
CG B:GLU87 4.3 36.5 1.0
CG B:GLU32 4.3 38.6 1.0
N B:GLU32 4.4 33.9 1.0
OE1 B:GLN307 4.4 45.0 1.0
O B:SER30 4.4 33.9 1.0
CA B:ILE31 4.5 32.1 1.0
CD B:GLU311 4.5 52.1 1.0
OE1 B:GLU311 4.7 47.1 1.0
O B:LEU85 4.7 37.5 1.0
CB B:GLU32 4.8 35.8 1.0
OE2 B:GLU32 4.8 52.5 1.0
N B:GLU87 4.8 30.9 1.0
C B:ILE31 4.9 35.7 1.0

Reference:

M.A.Trevino, K.A.Amankwah, D.Fernandez, S.A.Weston, C.J.Stewart, J.M.Gallardo, M.Shahgholi, N.G.Sharaf. Expression, Purification, and Characterization of Diacylated Lipo-Ycjn From Escherichia Coli J.Biol.Chem. 2024.
ISSN: ESSN 1083-351X
DOI: 10.1016/J.JBC.2024.107853
Page generated: Thu Oct 31 21:34:57 2024

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