Potassium in PDB 6nuy: Structural Basis For Anti-Alpha-Galactosyl Response

Protein crystallography data

The structure of Structural Basis For Anti-Alpha-Galactosyl Response, PDB code: 6nuy was solved by D.B.Langley, D.Christ, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.31 / 1.55
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 101.492, 101.492, 78.159, 90.00, 90.00, 120.00
R / Rfree (%) 17.8 / 20.2

Potassium Binding Sites:

The binding sites of Potassium atom in the Structural Basis For Anti-Alpha-Galactosyl Response (pdb code 6nuy). 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 Structural Basis For Anti-Alpha-Galactosyl Response, PDB code: 6nuy:

Potassium binding site 1 out of 1 in 6nuy

Go back to Potassium Binding Sites List in 6nuy
Potassium binding site 1 out of 1 in the Structural Basis For Anti-Alpha-Galactosyl Response


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structural Basis For Anti-Alpha-Galactosyl Response within 5.0Å range:
probe atom residue distance (Å) B Occ
L:K301

b:28.9
occ:1.00
O L:HOH491 2.6 35.0 1.0
O L:LEU206 2.7 22.5 1.0
O L:HOH543 2.8 25.0 1.0
O L:GLN204 2.8 19.9 1.0
C L:GLN204 3.6 19.8 1.0
O L:HIS203 3.6 20.4 1.0
C L:LEU206 3.7 23.0 1.0
CA L:GLN204 3.9 19.0 1.0
O L:HOH526 4.2 23.3 1.0
CA L:SER207 4.3 25.1 0.5
N L:LEU206 4.3 21.1 1.0
CA L:SER207 4.3 25.8 0.5
N L:SER207 4.4 23.8 0.5
N L:SER207 4.4 24.2 0.5
O L:HOH447 4.4 42.6 1.0
C L:HIS203 4.5 19.5 1.0
O L:SER207 4.5 26.1 0.5
N L:GLY205 4.6 19.1 1.0
O L:SER207 4.6 25.9 0.5
C L:SER207 4.6 24.5 0.5
C L:SER207 4.6 24.2 0.5
N L:GLN204 4.6 18.9 1.0
CA L:LEU206 4.6 21.6 1.0
O L:HOH552 4.7 26.2 1.0
C L:GLY205 4.8 19.7 1.0

Reference:

D.B.Langley, D.Christ. Genetic and Structural Basis For the Human Anti-Alpha-Galactosyl Response To Be Published.
Page generated: Mon Dec 14 01:01:51 2020

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