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Potassium in PDB 5j9p: Kcsa in Vitro

Protein crystallography data

The structure of Kcsa in Vitro, PDB code: 5j9p was solved by K.Matulef, F.I.Valiyaveetil, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.64 / 2.85
Space group I 4
Cell size a, b, c (Å), α, β, γ (°) 155.695, 155.695, 74.791, 90.00, 90.00, 90.00
R / Rfree (%) 21.7 / 26.6

Potassium Binding Sites:

The binding sites of Potassium atom in the Kcsa in Vitro (pdb code 5j9p). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 6 binding sites of Potassium where determined in the Kcsa in Vitro, PDB code: 5j9p:
Jump to Potassium binding site number: 1; 2; 3; 4; 5; 6;

Potassium binding site 1 out of 6 in 5j9p

Go back to Potassium Binding Sites List in 5j9p
Potassium binding site 1 out of 6 in the Kcsa in Vitro


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Kcsa in Vitro within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K201

b:30.0
occ:0.25
O C:HOH307 4.0 45.1 1.0
K C:K202 4.2 30.0 0.2
O C:TYR78 4.2 33.7 1.0
CA C:GLY79 4.5 17.3 1.0
O C:GLY79 4.8 24.7 1.0
C C:GLY79 4.9 29.0 1.0

Potassium binding site 2 out of 6 in 5j9p

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Potassium binding site 2 out of 6 in the Kcsa in Vitro


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Kcsa in Vitro within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K202

b:30.0
occ:0.25
O C:TYR78 2.1 33.7 1.0
C C:TYR78 3.2 42.9 1.0
O C:GLY77 3.4 44.7 1.0
K C:K203 3.9 30.0 0.2
CA C:TYR78 4.0 25.7 1.0
N C:GLY79 4.1 33.6 1.0
K C:K201 4.2 30.0 0.2
CA C:GLY79 4.2 17.3 1.0
C C:GLY77 4.4 37.1 1.0
N C:TYR78 4.7 20.7 1.0

Potassium binding site 3 out of 6 in 5j9p

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Potassium binding site 3 out of 6 in the Kcsa in Vitro


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Kcsa in Vitro within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K203

b:30.0
occ:0.25
K C:K204 2.7 30.0 0.2
O C:VAL76 2.7 69.0 1.0
O C:GLY77 2.9 44.7 1.0
C C:GLY77 3.7 37.1 1.0
K C:K202 3.9 30.0 0.2
C C:VAL76 3.9 33.5 1.0
CA C:GLY77 4.3 41.6 1.0
N C:GLY77 4.6 25.3 1.0
N C:TYR78 4.6 20.7 1.0
O C:TYR78 4.8 33.7 1.0
CA C:TYR78 4.9 25.7 1.0
O C:THR75 5.0 63.1 1.0

Potassium binding site 4 out of 6 in 5j9p

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Potassium binding site 4 out of 6 in the Kcsa in Vitro


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Kcsa in Vitro within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K204

b:30.0
occ:0.25
O C:VAL76 2.6 69.0 1.0
K C:K203 2.7 30.0 0.2
O C:THR75 2.9 63.1 1.0
C C:VAL76 3.5 33.5 1.0
C C:THR75 4.0 30.8 1.0
CA C:VAL76 4.0 29.1 1.0
K C:K205 4.1 30.0 0.2
N C:VAL76 4.5 23.8 1.0
N C:GLY77 4.6 25.3 1.0
O C:GLY77 4.9 44.7 1.0

Potassium binding site 5 out of 6 in 5j9p

Go back to Potassium Binding Sites List in 5j9p
Potassium binding site 5 out of 6 in the Kcsa in Vitro


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 5 of Kcsa in Vitro within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K205

b:30.0
occ:0.25
OG1 C:THR75 2.7 33.4 1.0
O C:THR75 3.2 63.1 1.0
CB C:THR75 3.5 38.5 1.0
C C:THR75 4.0 30.8 1.0
K C:K204 4.1 30.0 0.2
CA C:THR75 4.4 34.3 1.0
CG2 C:THR75 4.6 28.5 1.0
O C:THR74 4.8 39.8 1.0
N C:VAL76 5.0 23.8 1.0

Potassium binding site 6 out of 6 in 5j9p

Go back to Potassium Binding Sites List in 5j9p
Potassium binding site 6 out of 6 in the Kcsa in Vitro


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 6 of Kcsa in Vitro within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K206

b:30.0
occ:0.25
O C:HOH306 3.6 39.6 1.0
O C:HOH303 4.0 31.8 1.0

Reference:

P.J.Focke, C.Hein, B.Hoffmann, K.Matulef, F.Bernhard, V.Dotsch, F.I.Valiyaveetil. Combining in Vitro Folding with Cell Free Protein Synthesis For Membrane Protein Expression. Biochemistry V. 55 4212 2016.
ISSN: ISSN 0006-2960
PubMed: 27384110
DOI: 10.1021/ACS.BIOCHEM.6B00488
Page generated: Sat Aug 9 09:18:42 2025

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