Potassium in PDB 2a79: Mammalian Shaker KV1.2 Potassium Channel- Beta Subunit Complex

The structure of Mammalian Shaker KV1.2 Potassium Channel- Beta Subunit Complex, PDB code: 2a79 was solved by S.B.Long, E.B.Campbell, R.Mackinnon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.48 / 2.90
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	113.605, 113.605, 260.473, 90.00, 90.00, 90.00
R / Rfree (%)	22.2 / 25.2

The binding sites of Potassium atom in the Mammalian Shaker KV1.2 Potassium Channel- Beta Subunit Complex (pdb code 2a79). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 6 binding sites of Potassium where determined in the Mammalian Shaker KV1.2 Potassium Channel- Beta Subunit Complex, PDB code: 2a79:
Jump to Potassium binding site number: 1; 2; 3; 4; 5; 6;

Potassium binding site 1 out of 6 in the Mammalian Shaker KV1.2 Potassium Channel- Beta Subunit Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Mammalian Shaker KV1.2 Potassium Channel- Beta Subunit Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:K500 b:89.2 occ:0.50 O B:TYR377 3.2 0.5 1.0 O B:GLY376 3.2 0.0 1.0 K B:K501 3.4 89.2 0.5 C B:TYR377 3.6 0.4 1.0 N B:GLY378 4.1 0.6 1.0 CA B:TYR377 4.2 0.1 1.0 C B:GLY376 4.2 0.1 1.0 CA B:GLY378 4.4 0.7 1.0 K B:K505 4.5 89.2 0.5 N B:TYR377 4.7 0.2 1.0

Potassium binding site 2 out of 6 in the Mammalian Shaker KV1.2 Potassium Channel- Beta Subunit Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Mammalian Shaker KV1.2 Potassium Channel- Beta Subunit Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:K501 b:89.2 occ:0.50 O B:VAL375 3.0 0.3 1.0 O B:GLY376 3.2 0.0 1.0 K B:K502 3.2 89.2 0.5 K B:K500 3.4 89.2 0.5 C B:GLY376 3.7 0.1 1.0 C B:VAL375 4.0 0.5 1.0 CA B:GLY376 4.1 0.9 1.0 N B:GLY376 4.5 0.7 1.0 N B:TYR377 4.6 0.2 1.0 CA B:TYR377 5.0 0.1 1.0

Potassium binding site 3 out of 6 in the Mammalian Shaker KV1.2 Potassium Channel- Beta Subunit Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Mammalian Shaker KV1.2 Potassium Channel- Beta Subunit Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:K502 b:89.2 occ:0.50 O B:THR374 2.9 0.3 1.0 K B:K501 3.2 89.2 0.5 O B:VAL375 3.3 0.3 1.0 K B:K503 3.3 89.2 0.5 C B:VAL375 3.8 0.5 1.0 C B:THR374 4.0 0.4 1.0 CA B:VAL375 4.1 0.5 1.0 N B:VAL375 4.5 0.6 1.0 N B:GLY376 4.7 0.7 1.0

Potassium binding site 4 out of 6 in the Mammalian Shaker KV1.2 Potassium Channel- Beta Subunit Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Mammalian Shaker KV1.2 Potassium Channel- Beta Subunit Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:K503 b:89.2 occ:0.50 OG1 B:THR374 3.1 0.7 1.0 O B:THR374 3.2 0.3 1.0 K B:K502 3.3 89.2 0.5 CB B:THR374 3.8 1.0 1.0 C B:THR374 4.1 0.4 1.0 CA B:THR374 4.6 0.1 1.0 CG2 B:THR374 4.9 0.0 1.0 O B:THR373 4.9 0.8 1.0

Potassium binding site 5 out of 6 in the Mammalian Shaker KV1.2 Potassium Channel- Beta Subunit Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 5 of Mammalian Shaker KV1.2 Potassium Channel- Beta Subunit Complex within 5.0Å range:

Potassium binding site 6 out of 6 in the Mammalian Shaker KV1.2 Potassium Channel- Beta Subunit Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 6 of Mammalian Shaker KV1.2 Potassium Channel- Beta Subunit Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:K505 b:89.2 occ:0.50 O B:TYR377 4.3 0.5 1.0 K B:K500 4.5 89.2 0.5 CA B:GLY378 4.8 0.7 1.0 O B:GLY378 4.8 0.6 1.0

S.B.Long, E.B.Campbell, R.Mackinnon. Crystal Structure of A Mammalian Voltage-Dependent Shaker Family K+ Channel. Science V. 309 897 2005.
ISSN: ISSN 0036-8075
PubMed: 16002581
DOI: 10.1126/SCIENCE.1116269