Potassium in PDB 4jtd: Crystal Structure of KV1.2-2.1 Paddle Chimera Channel in Complex with LYS27MET Mutant of Charybdotoxin

The structure of Crystal Structure of KV1.2-2.1 Paddle Chimera Channel in Complex with LYS27MET Mutant of Charybdotoxin, PDB code: 4jtd was solved by A.Banerjee, A.Lee, E.Campbell, R.Mackinnon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.54
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	144.867, 144.867, 284.292, 90.00, 90.00, 90.00
R / Rfree (%)	21 / 23.5

The binding sites of Potassium atom in the Crystal Structure of KV1.2-2.1 Paddle Chimera Channel in Complex with LYS27MET Mutant of Charybdotoxin (pdb code 4jtd). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 8 binding sites of Potassium where determined in the Crystal Structure of KV1.2-2.1 Paddle Chimera Channel in Complex with LYS27MET Mutant of Charybdotoxin, PDB code: 4jtd:
Jump to Potassium binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Potassium binding site 1 out of 8 in the Crystal Structure of KV1.2-2.1 Paddle Chimera Channel in Complex with LYS27MET Mutant of Charybdotoxin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of KV1.2-2.1 Paddle Chimera Channel in Complex with LYS27MET Mutant of Charybdotoxin within 5.0Å range: probe atom residue distance (Å) B Occ B:K501 b:42.6 occ:0.50 O B:TYR373 3.1 44.3 1.0 O B:GLY372 3.7 42.9 1.0 C B:TYR373 3.7 43.5 1.0 K B:K502 3.8 39.8 0.5 N B:GLY374 4.4 44.2 1.0 CA B:GLY374 4.4 43.4 1.0 CA B:TYR373 4.5 42.8 1.0 C B:GLY372 4.8 43.4 1.0

Potassium binding site 2 out of 8 in the Crystal Structure of KV1.2-2.1 Paddle Chimera Channel in Complex with LYS27MET Mutant of Charybdotoxin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of KV1.2-2.1 Paddle Chimera Channel in Complex with LYS27MET Mutant of Charybdotoxin within 5.0Å range: probe atom residue distance (Å) B Occ B:K502 b:39.8 occ:0.50 O B:GLY372 3.2 42.9 1.0 K B:K503 3.2 34.0 0.5 O B:VAL371 3.3 45.0 1.0 C B:GLY372 3.7 43.4 1.0 K B:K501 3.8 42.6 0.5 CA B:GLY372 4.2 42.4 1.0 C B:VAL371 4.3 43.5 1.0 N B:TYR373 4.6 42.6 1.0 N B:GLY372 4.7 43.5 1.0 CA B:TYR373 4.9 42.8 1.0

Potassium binding site 3 out of 8 in the Crystal Structure of KV1.2-2.1 Paddle Chimera Channel in Complex with LYS27MET Mutant of Charybdotoxin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Crystal Structure of KV1.2-2.1 Paddle Chimera Channel in Complex with LYS27MET Mutant of Charybdotoxin within 5.0Å range: probe atom residue distance (Å) B Occ B:K503 b:34.0 occ:0.50 O B:THR370 3.2 40.4 1.0 K B:K502 3.2 39.8 0.5 O B:VAL371 3.3 45.0 1.0 C B:VAL371 3.8 43.5 1.0 K B:K504 3.9 39.6 0.5 CA B:VAL371 4.2 42.1 1.0 C B:THR370 4.3 41.1 1.0 N B:GLY372 4.6 43.5 1.0 N B:VAL371 4.7 42.4 1.0 CA B:GLY372 4.9 42.4 1.0

Potassium binding site 4 out of 8 in the Crystal Structure of KV1.2-2.1 Paddle Chimera Channel in Complex with LYS27MET Mutant of Charybdotoxin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Crystal Structure of KV1.2-2.1 Paddle Chimera Channel in Complex with LYS27MET Mutant of Charybdotoxin within 5.0Å range: probe atom residue distance (Å) B Occ B:K504 b:39.6 occ:0.50 OG1 B:THR370 3.2 42.3 1.0 O B:THR370 3.4 40.4 1.0 K B:K503 3.9 34.0 0.5 CB B:THR370 4.0 43.1 1.0 C B:THR370 4.3 41.1 1.0 CA B:THR370 4.8 41.9 1.0

Potassium binding site 5 out of 8 in the Crystal Structure of KV1.2-2.1 Paddle Chimera Channel in Complex with LYS27MET Mutant of Charybdotoxin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 5 of Crystal Structure of KV1.2-2.1 Paddle Chimera Channel in Complex with LYS27MET Mutant of Charybdotoxin within 5.0Å range: probe atom residue distance (Å) B Occ H:K501 b:53.6 occ:0.50 O H:TYR373 3.4 95.5 1.0 K H:K502 3.6 55.9 0.5 O H:GLY372 3.6 93.1 1.0 C H:TYR373 3.8 95.4 1.0 N H:GLY374 4.2 97.2 1.0 CA H:GLY374 4.3 98.6 1.0 SD Y:MET27 4.5 80.3 0.2 CA H:TYR373 4.5 93.8 1.0 C H:GLY372 4.6 93.4 1.0 N H:TYR373 5.0 93.7 1.0

Potassium binding site 6 out of 8 in the Crystal Structure of KV1.2-2.1 Paddle Chimera Channel in Complex with LYS27MET Mutant of Charybdotoxin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 6 of Crystal Structure of KV1.2-2.1 Paddle Chimera Channel in Complex with LYS27MET Mutant of Charybdotoxin within 5.0Å range: probe atom residue distance (Å) B Occ H:K502 b:55.9 occ:0.50 O H:GLY372 3.3 93.1 1.0 O H:VAL371 3.4 89.5 1.0 K H:K501 3.6 53.6 0.5 C H:GLY372 3.6 93.4 1.0 K H:K503 3.7 56.2 0.5 CA H:GLY372 4.0 92.7 1.0 C H:VAL371 4.3 89.7 1.0 N H:TYR373 4.4 93.7 1.0 N H:GLY372 4.6 91.5 1.0 CA H:TYR373 4.9 93.8 1.0

Potassium binding site 7 out of 8 in the Crystal Structure of KV1.2-2.1 Paddle Chimera Channel in Complex with LYS27MET Mutant of Charybdotoxin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 7 of Crystal Structure of KV1.2-2.1 Paddle Chimera Channel in Complex with LYS27MET Mutant of Charybdotoxin within 5.0Å range: probe atom residue distance (Å) B Occ H:K503 b:56.2 occ:0.50 O H:THR370 3.2 85.9 1.0 O H:VAL371 3.4 89.5 1.0 K H:K504 3.5 56.0 0.5 K H:K502 3.7 55.9 0.5 C H:VAL371 3.9 89.7 1.0 C H:THR370 4.3 85.7 1.0 CA H:VAL371 4.3 88.1 1.0 N H:GLY372 4.6 91.5 1.0 N H:VAL371 4.8 86.8 1.0 CA H:GLY372 4.9 92.7 1.0

Potassium binding site 8 out of 8 in the Crystal Structure of KV1.2-2.1 Paddle Chimera Channel in Complex with LYS27MET Mutant of Charybdotoxin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 8 of Crystal Structure of KV1.2-2.1 Paddle Chimera Channel in Complex with LYS27MET Mutant of Charybdotoxin within 5.0Å range: probe atom residue distance (Å) B Occ H:K504 b:56.0 occ:0.50 OG1 H:THR370 3.4 82.0 1.0 O H:THR370 3.5 85.9 1.0 K H:K503 3.5 56.2 0.5 CB H:THR370 4.2 83.6 1.0 C H:THR370 4.5 85.7 1.0

A.Banerjee, A.Lee, E.Campbell, R.Mackinnon. Structure of A Pore-Blocking Toxin in Complex with A Eukaryotic Voltage-Dependent K(+) Channel. Elife V. 2 00594 2013.
ISSN: ESSN 2050-084X
PubMed: 23705070
DOI: 10.7554/ELIFE.00594