Potassium in PDB 3hpl: Kcsa E71H-F103A Mutant in the Closed State

The structure of Kcsa E71H-F103A Mutant in the Closed State, PDB code: 3hpl was solved by L.G.Cuello, V.Jogini, D.M.Cortes, E.Perozo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 3.20
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	156.140, 156.140, 76.292, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 26.9

The binding sites of Potassium atom in the Kcsa E71H-F103A Mutant in the Closed State (pdb code 3hpl). 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 E71H-F103A Mutant in the Closed State, PDB code: 3hpl:
Jump to Potassium binding site number: 1; 2; 3; 4; 5; 6;

Potassium binding site 1 out of 6 in the Kcsa E71H-F103A Mutant in the Closed State


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Kcsa E71H-F103A Mutant in the Closed State within 5.0Å range: probe atom residue distance (Å) B Occ C:K3001 b:75.8 occ:0.25 O C:TYR78 3.0 40.6 1.0 K C:K3002 3.4 0.7 0.3 C C:TYR78 3.6 40.9 1.0 O C:GLY77 3.8 40.4 1.0 CA C:TYR78 4.3 39.6 1.0 K C:K3007 4.3 78.4 0.2 N C:GLY79 4.4 42.5 1.0 CA C:GLY79 4.6 42.5 1.0 C C:GLY77 4.8 40.4 1.0

Potassium binding site 2 out of 6 in the Kcsa E71H-F103A Mutant in the Closed State


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Kcsa E71H-F103A Mutant in the Closed State within 5.0Å range: probe atom residue distance (Å) B Occ C:K3003 b:97.8 occ:0.25 O C:THR75 3.1 38.6 1.0 K C:K3002 3.3 0.7 0.3 K C:K3004 3.3 38.4 0.2 O C:VAL76 3.5 37.8 1.0 C C:VAL76 3.9 36.6 1.0 CA C:VAL76 4.1 34.5 1.0 C C:THR75 4.1 37.8 1.0 N C:VAL76 4.6 36.4 1.0 N C:GLY77 4.8 39.2 1.0

Potassium binding site 3 out of 6 in the Kcsa E71H-F103A Mutant in the Closed State


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Kcsa E71H-F103A Mutant in the Closed State within 5.0Å range: probe atom residue distance (Å) B Occ C:K3004 b:38.4 occ:0.25 O C:THR75 2.8 38.6 1.0 K C:K3003 3.3 97.8 0.2 OG1 C:THR75 3.4 32.2 1.0 C C:THR75 3.9 37.8 1.0 CB C:THR75 3.9 34.6 1.0 CA C:THR75 4.7 37.0 1.0 N C:VAL76 4.9 36.4 1.0

Potassium binding site 4 out of 6 in the Kcsa E71H-F103A Mutant in the Closed State


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Kcsa E71H-F103A Mutant in the Closed State within 5.0Å range:

Potassium binding site 5 out of 6 in the Kcsa E71H-F103A Mutant in the Closed State


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 5 of Kcsa E71H-F103A Mutant in the Closed State within 5.0Å range: probe atom residue distance (Å) B Occ C:K3002 b:0.7 occ:0.25 O C:GLY77 3.1 40.4 1.0 K C:K3003 3.3 97.8 0.2 O C:VAL76 3.4 37.8 1.0 K C:K3001 3.4 75.8 0.2 C C:GLY77 4.0 40.4 1.0 C C:VAL76 4.4 36.6 1.0 CA C:GLY77 4.7 40.4 1.0 N C:TYR78 4.7 40.2 1.0 CA C:TYR78 4.8 39.6 1.0 N C:GLY77 5.0 39.2 1.0

Potassium binding site 6 out of 6 in the Kcsa E71H-F103A Mutant in the Closed State


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 6 of Kcsa E71H-F103A Mutant in the Closed State within 5.0Å range: probe atom residue distance (Å) B Occ C:K3007 b:78.4 occ:0.25 K C:K3001 4.3 75.8 0.2 O C:TYR78 4.3 40.6 1.0

L.G.Cuello, V.Jogini, D.M.Cortes, A.C.Pan, D.G.Gagnon, O.Dalmas, J.F.Cordero-Morales, S.Chakrapani, B.Roux, E.Perozo. Structural Basis For the Coupling Between Activation and Inactivation Gates in K(+) Channels. Nature V. 466 272 2010.
ISSN: ISSN 0028-0836
PubMed: 20613845
DOI: 10.1038/NATURE09136