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Potassium in PDB 9cko: Human G Protein-Coupled Receptor Kinase 5 Wild-Type in Complex with Sangivamycin

Enzymatic activity of Human G Protein-Coupled Receptor Kinase 5 Wild-Type in Complex with Sangivamycin

All present enzymatic activity of Human G Protein-Coupled Receptor Kinase 5 Wild-Type in Complex with Sangivamycin:
2.7.11.16;

Protein crystallography data

The structure of Human G Protein-Coupled Receptor Kinase 5 Wild-Type in Complex with Sangivamycin, PDB code: 9cko was solved by Y.Chen, J.J.G.Tesmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.45 / 2.80
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 140.259, 140.259, 78.766, 90, 90, 90
R / Rfree (%) 24 / 28

Potassium Binding Sites:

The binding sites of Potassium atom in the Human G Protein-Coupled Receptor Kinase 5 Wild-Type in Complex with Sangivamycin (pdb code 9cko). 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 Human G Protein-Coupled Receptor Kinase 5 Wild-Type in Complex with Sangivamycin, PDB code: 9cko:

Potassium binding site 1 out of 1 in 9cko

Go back to Potassium Binding Sites List in 9cko
Potassium binding site 1 out of 1 in the Human G Protein-Coupled Receptor Kinase 5 Wild-Type in Complex with Sangivamycin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Human G Protein-Coupled Receptor Kinase 5 Wild-Type in Complex with Sangivamycin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K603

b:50.2
occ:1.00
O A:ASN280 2.7 58.1 1.0
O A:HOH759 2.8 55.1 1.0
O A:HIS274 2.9 51.6 1.0
O A:GLY282 3.0 58.7 1.0
O A:HOH735 3.0 48.8 1.0
O A:MET278 3.0 49.4 1.0
HA A:ILE275 3.3 70.1 1.0
O A:ILE275 3.4 56.6 1.0
C A:GLY282 3.7 53.7 1.0
HB3 A:PHE283 3.8 73.9 1.0
C A:ILE275 3.8 56.1 1.0
HD2 A:PHE283 3.8 62.8 1.0
H A:GLY282 3.8 67.4 1.0
CA A:ILE275 3.9 57.8 1.0
C A:HIS274 3.9 54.2 1.0
C A:MET278 4.0 49.3 1.0
C A:ASN280 4.0 59.3 1.0
N A:GLY282 4.0 55.6 1.0
O A:HOH730 4.1 47.8 1.0
HB2 A:MET278 4.1 62.8 1.0
H A:MET278 4.2 58.3 1.0
CA A:GLY282 4.3 53.8 1.0
HA A:PHE283 4.3 66.3 1.0
N A:ILE275 4.4 58.2 1.0
HA A:PRO281 4.4 68.2 1.0
C A:PRO281 4.4 59.2 1.0
N A:PHE283 4.4 54.5 1.0
N A:ASN280 4.5 59.3 1.0
HA2 A:GLY282 4.5 65.3 1.0
HA3 A:GLY279 4.5 59.6 1.0
C A:GLY279 4.6 53.2 1.0
HH12 A:ARG287 4.6 69.2 1.0
CB A:PHE283 4.6 61.0 1.0
H A:ASN280 4.6 71.8 1.0
CD2 A:PHE283 4.6 51.8 1.0
HB3 A:MET278 4.6 62.8 1.0
CA A:PHE283 4.7 54.7 1.0
CB A:MET278 4.7 51.8 1.0
N A:GLY279 4.7 52.0 1.0
CA A:MET278 4.7 46.6 1.0
CA A:PRO281 4.8 56.3 1.0
N A:TYR276 4.8 60.5 1.0
CA A:GLY279 4.8 49.1 1.0
N A:PRO281 4.8 59.1 1.0
CA A:ASN280 4.9 61.8 1.0
N A:MET278 4.9 48.0 1.0
O A:GLY279 4.9 47.4 1.0
HG23 A:ILE275 5.0 84.4 1.0

Reference:

Y.Chen, J.J.G.Tesmer. Structures of G Protein-Coupled Receptor Kinase 5 in Multiple Conformations Reveals Mechanism of Activation and Inhibition To Be Published.
Page generated: Sat Aug 9 18:35:27 2025

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