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Potassium in PDB 6rv2: Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation

Protein crystallography data

The structure of Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation, PDB code: 6rv2 was solved by K.E.J.Rodstrom, A.C.W.Pike, W.Zhang, A.Quigley, D.Speedman, S.M.M.Mukhopadhyay, L.Shrestha, R.Chalk, S.Venkaya, S.R.Bushell, A.Tessitore, N.Burgess-Brown, C.H.Arrowsmith, A.M.Edwards, C.Bountra, E.P.Carpenter, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.04 / 3.00
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.140, 204.790, 238.340, 90.00, 90.00, 90.00
R / Rfree (%) 25.3 / 25.7

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation (pdb code 6rv2). 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 the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation, PDB code: 6rv2:
Jump to Potassium binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Potassium binding site 1 out of 8 in 6rv2

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Potassium binding site 1 out of 8 in the Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation


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 the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K302

b:43.2
occ:1.00
 O A:ILE94 2.7 37.9 1.0
O A:GLY201 2.7 36.3 1.0
O B:ILE94 2.7 35.4 1.0
O A:ILE200 2.7 33.1 1.0
O A:GLY95 2.7 39.6 1.0
O B:ILE200 2.7 39.0 1.0
O B:GLY201 2.8 38.1 1.0
K A:K303 2.8 33.2 1.0
O B:GLY95 2.8 37.7 1.0
K A:K309 3.1 33.4 1.0
C A:GLY201 3.6 36.6 1.0
C A:GLY95 3.6 39.2 1.0
C B:GLY201 3.6 37.9 1.0
C B:GLY95 3.6 37.9 1.0
C A:ILE94 3.8 37.6 1.0
C B:ILE94 3.9 35.8 1.0
C A:ILE200 3.9 33.4 1.0
C B:ILE200 3.9 38.9 1.0
CA A:GLY201 4.1 31.0 1.0
CA B:GLY201 4.1 34.9 1.0
CA A:GLY95 4.2 33.8 1.0
CA B:GLY95 4.2 33.3 1.0
N A:GLY201 4.4 30.7 1.0
N A:GLY95 4.4 33.8 1.0
N B:GLY201 4.4 35.4 1.0
N B:GLY95 4.4 32.8 1.0
N A:TYR96 4.5 35.5 1.0
N A:PHE202 4.6 34.4 1.0
N B:TYR96 4.6 34.3 1.0
N B:PHE202 4.6 33.2 1.0
O B:THR93 4.8 33.0 1.0
CA A:TYR96 4.8 35.0 1.0
O A:THR93 4.8 38.6 1.0
CA B:TYR96 4.9 34.3 1.0
O A:THR199 4.9 35.1 1.0
O B:THR199 4.9 34.3 1.0
CA A:PHE202 4.9 34.9 1.0
CA B:PHE202 4.9 32.3 1.0

Potassium binding site 2 out of 8 in 6rv2

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Potassium binding site 2 out of 8 in the Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation


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 the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K303

b:33.2
occ:1.00
 O B:THR93 2.6 33.0 1.0
O A:THR93 2.7 38.6 1.0
O A:THR199 2.7 35.1 1.0
O B:THR199 2.7 34.3 1.0
O A:ILE200 2.7 33.1 1.0
O B:ILE200 2.8 39.0 1.0
K A:K302 2.8 43.2 1.0
O B:ILE94 2.8 35.4 1.0
O A:ILE94 2.8 37.9 1.0
K A:K304 3.5 40.2 1.0
C A:ILE200 3.6 33.4 1.0
C B:ILE200 3.6 38.9 1.0
C B:ILE94 3.6 35.8 1.0
C A:ILE94 3.6 37.6 1.0
C B:THR93 3.8 34.8 1.0
C A:THR93 3.8 38.5 1.0
C A:THR199 3.8 34.6 1.0
C B:THR199 3.8 35.0 1.0
CA B:ILE94 4.1 31.4 1.0
CA A:ILE94 4.1 32.2 1.0
CA A:ILE200 4.1 28.1 1.0
CA B:ILE200 4.1 33.5 1.0
N B:ILE94 4.4 31.5 1.0
N A:ILE200 4.4 29.3 1.0
N B:ILE200 4.4 32.9 1.0
N A:ILE94 4.4 32.8 1.0
N B:GLY95 4.5 32.8 1.0
N A:GLY201 4.5 30.7 1.0
N B:GLY201 4.5 35.4 1.0
N A:GLY95 4.5 33.8 1.0
O A:GLY95 4.8 39.6 1.0
O A:GLY201 4.8 36.3 1.0
O B:GLY95 4.8 37.7 1.0
O B:GLY201 4.8 38.1 1.0
CA A:GLY201 4.9 31.0 1.0
CA B:GLY201 4.9 34.9 1.0
CA B:THR93 5.0 32.7 1.0
CA B:GLY95 5.0 33.3 1.0
CA A:GLY95 5.0 33.8 1.0

Potassium binding site 3 out of 8 in 6rv2

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Potassium binding site 3 out of 8 in the Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation


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 the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K304

b:40.2
occ:1.00
 O A:THR199 2.7 35.1 1.0
OG1 A:THR199 2.7 30.4 1.0
OG1 B:THR93 2.7 28.2 1.0
OG1 A:THR93 2.8 33.1 1.0
O B:THR93 2.9 33.0 1.0
O A:THR93 2.9 38.6 1.0
O B:THR199 2.9 34.3 1.0
OG1 B:THR199 3.0 30.5 1.0
CB B:THR93 3.3 31.8 1.0
CB A:THR199 3.3 34.8 1.0
CB A:THR93 3.4 36.4 1.0
K A:K303 3.5 33.2 1.0
CB B:THR199 3.6 32.1 1.0
C A:THR199 3.6 34.6 1.0
C B:THR93 3.7 34.8 1.0
C A:THR93 3.8 38.5 1.0
C B:THR199 3.9 35.0 1.0
CA A:THR199 4.1 31.1 1.0
CA B:THR93 4.1 32.7 1.0
CA A:THR93 4.2 36.1 1.0
CA B:THR199 4.3 30.6 1.0
CG2 B:THR93 4.4 25.5 1.0
CG2 A:THR199 4.5 34.2 1.0
CG2 A:THR93 4.6 34.6 1.0
N A:ILE200 4.7 29.3 1.0
CG2 B:THR199 4.8 29.6 1.0
N A:ILE94 4.8 32.8 1.0
N B:ILE94 4.8 31.5 1.0
O A:THR198 4.9 37.2 1.0
O A:THR92 4.9 42.5 1.0
N B:ILE200 4.9 32.9 1.0
O B:THR92 5.0 38.6 1.0

Potassium binding site 4 out of 8 in 6rv2

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Potassium binding site 4 out of 8 in the Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation


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 the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K309

b:33.4
occ:1.00
 O A:TYR96 2.8 41.2 1.0
O A:GLY201 2.8 36.3 1.0
O B:GLY201 2.8 38.1 1.0
O B:TYR96 2.8 41.4 1.0
O B:PHE202 2.8 39.4 1.0
O A:PHE202 2.9 40.5 1.0
O A:GLY95 2.9 39.6 1.0
O B:GLY95 2.9 37.7 1.0
K A:K302 3.1 43.2 1.0
C A:TYR96 3.4 41.6 1.0
C B:TYR96 3.4 41.7 1.0
C B:PHE202 3.5 38.3 1.0
C A:PHE202 3.5 39.7 1.0
CA A:TYR96 3.8 35.0 1.0
CA B:TYR96 3.9 34.3 1.0
C B:GLY201 3.9 37.9 1.0
C A:GLY201 3.9 36.6 1.0
C A:GLY95 3.9 39.2 1.0
CA B:PHE202 4.0 32.3 1.0
C B:GLY95 4.0 37.9 1.0
CA A:PHE202 4.0 34.9 1.0
N A:GLY97 4.3 40.6 1.0
N B:GLY97 4.3 40.8 1.0
N A:TYR96 4.3 35.5 1.0
N B:TYR96 4.4 34.3 1.0
N A:GLY203 4.4 36.0 1.0
N B:GLY203 4.4 35.2 1.0
N B:PHE202 4.4 33.2 1.0
N A:PHE202 4.4 34.4 1.0
CA A:GLY97 4.7 42.0 1.0
CA B:GLY97 4.8 41.7 1.0
CA A:GLY203 4.8 36.2 1.0
CA B:GLY203 4.8 35.6 1.0
O A:ILE94 5.0 37.9 1.0
O B:ILE94 5.0 35.4 1.0

Potassium binding site 5 out of 8 in 6rv2

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Potassium binding site 5 out of 8 in the Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation


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 the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K301

b:40.6
occ:1.00
 O C:GLY201 2.8 43.0 1.0
O C:TYR96 2.8 44.5 1.0
O D:TYR96 2.8 47.7 1.0
O D:GLY201 2.8 44.3 1.0
O D:PHE202 2.8 43.1 1.0
O C:GLY95 2.8 40.4 1.0
O C:PHE202 2.9 41.4 1.0
O D:GLY95 2.9 44.3 1.0
K C:K302 3.0 0.5 1.0
C C:TYR96 3.4 45.4 1.0
C D:TYR96 3.4 47.2 1.0
C C:PHE202 3.5 42.4 1.0
C D:PHE202 3.5 43.7 1.0
CA C:TYR96 3.8 40.1 1.0
CA D:TYR96 3.9 42.3 1.0
C C:GLY201 3.9 42.8 1.0
C C:GLY95 3.9 41.2 1.0
C D:GLY201 3.9 44.9 1.0
CA D:PHE202 4.0 38.9 1.0
CA C:PHE202 4.0 37.7 1.0
C D:GLY95 4.0 44.6 1.0
N C:GLY97 4.3 43.6 1.0
N D:GLY97 4.3 43.6 1.0
N C:TYR96 4.3 39.4 1.0
N C:GLY203 4.4 40.1 1.0
N D:TYR96 4.4 42.1 1.0
N C:PHE202 4.4 38.2 1.0
N D:GLY203 4.4 41.0 1.0
N D:PHE202 4.4 39.6 1.0
CA C:GLY97 4.8 44.4 1.0
CA D:GLY97 4.8 43.8 1.0
CA C:GLY203 4.8 40.4 1.0
CA D:GLY203 4.9 41.1 1.0
O C:ILE94 4.9 39.2 1.0

Potassium binding site 6 out of 8 in 6rv2

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Potassium binding site 6 out of 8 in the Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation


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 the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K302

b:0.5
occ:1.00
 O C:GLY201 2.7 43.0 1.0
O C:ILE94 2.7 39.2 1.0
O D:GLY201 2.7 44.3 1.0
O C:GLY95 2.7 40.4 1.0
O D:GLY95 2.7 44.3 1.0
O C:ILE200 2.8 41.9 1.0
O D:ILE94 2.8 41.5 1.0
O D:ILE200 2.8 48.8 1.0
K C:K303 2.8 37.2 1.0
K C:K301 3.0 40.6 1.0
C C:GLY201 3.6 42.8 1.0
C C:GLY95 3.6 41.2 1.0
C D:GLY201 3.6 44.9 1.0
C D:GLY95 3.6 44.6 1.0
C C:ILE94 3.8 39.6 1.0
C C:ILE200 3.9 42.3 1.0
C D:ILE94 3.9 41.1 1.0
C D:ILE200 3.9 47.6 1.0
CA C:GLY201 4.1 38.3 1.0
CA D:GLY201 4.1 42.9 1.0
CA C:GLY95 4.2 36.3 1.0
CA D:GLY95 4.2 39.4 1.0
N C:GLY201 4.4 38.2 1.0
N C:GLY95 4.4 36.5 1.0
N D:GLY201 4.4 43.5 1.0
N D:GLY95 4.5 39.0 1.0
N C:TYR96 4.5 39.4 1.0
N D:TYR96 4.5 42.1 1.0
N D:PHE202 4.6 39.6 1.0
N C:PHE202 4.6 38.2 1.0
CA C:TYR96 4.8 40.1 1.0
CA D:TYR96 4.8 42.3 1.0
O C:THR93 4.9 36.4 1.0
CA D:PHE202 4.9 38.9 1.0
O D:THR93 4.9 37.1 1.0
CA C:PHE202 4.9 37.7 1.0
O C:THR199 4.9 42.5 1.0
O D:THR199 5.0 45.9 1.0

Potassium binding site 7 out of 8 in 6rv2

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Potassium binding site 7 out of 8 in the Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation


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 the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K303

b:37.2
occ:1.00
 O C:THR93 2.7 36.4 1.0
O C:THR199 2.7 42.5 1.0
O D:THR93 2.7 37.1 1.0
O D:ILE200 2.7 48.8 1.0
O D:THR199 2.7 45.9 1.0
O C:ILE200 2.8 41.9 1.0
K C:K302 2.8 0.5 1.0
O C:ILE94 2.8 39.2 1.0
O D:ILE94 2.8 41.5 1.0
C D:ILE200 3.5 47.6 1.0
C C:ILE94 3.6 39.6 1.0
C C:ILE200 3.6 42.3 1.0
K C:K304 3.6 44.6 1.0
C D:ILE94 3.6 41.1 1.0
C C:THR93 3.8 37.2 1.0
C C:THR199 3.8 42.8 1.0
C D:THR199 3.9 46.4 1.0
C D:THR93 3.9 37.8 1.0
CA C:ILE94 4.0 34.6 1.0
CA D:ILE200 4.1 41.9 1.0
CA C:ILE200 4.1 38.5 1.0
CA D:ILE94 4.1 34.3 1.0
N C:ILE94 4.4 34.8 1.0
N C:ILE200 4.4 39.0 1.0
N D:ILE200 4.4 42.4 1.0
N D:ILE94 4.4 34.1 1.0
N C:GLY95 4.5 36.5 1.0
N D:GLY201 4.5 43.5 1.0
N C:GLY201 4.5 38.2 1.0
N D:GLY95 4.5 39.0 1.0
O D:GLY95 4.8 44.3 1.0
O C:GLY95 4.8 40.4 1.0
O D:GLY201 4.8 44.3 1.0
O C:GLY201 4.8 43.0 1.0
CA D:GLY201 4.9 42.9 1.0
CA C:GLY201 4.9 38.3 1.0
CA C:GLY95 5.0 36.3 1.0
CA D:GLY95 5.0 39.4 1.0
CA C:THR93 5.0 33.7 1.0

Potassium binding site 8 out of 8 in 6rv2

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Potassium binding site 8 out of 8 in the Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation


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 the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K304

b:44.6
occ:1.00
 OG1 D:THR93 2.7 42.5 1.0
O C:THR199 2.8 42.5 1.0
OG1 C:THR199 2.8 38.5 1.0
OG1 C:THR93 2.8 45.4 1.0
O D:THR199 2.8 45.9 1.0
O D:THR93 2.9 37.1 1.0
O C:THR93 2.9 36.4 1.0
OG1 D:THR199 2.9 51.1 1.0
CB D:THR93 3.3 46.0 1.0
CB C:THR199 3.3 40.4 1.0
CB C:THR93 3.4 43.8 1.0
CB D:THR199 3.5 48.9 1.0
K C:K303 3.6 37.2 1.0
C C:THR199 3.7 42.8 1.0
C D:THR93 3.7 37.8 1.0
C C:THR93 3.8 37.2 1.0
C D:THR199 3.8 46.4 1.0
CA C:THR199 4.1 38.6 1.0
CA D:THR93 4.1 35.7 1.0
CA C:THR93 4.2 33.7 1.0
CA D:THR199 4.2 43.0 1.0
CG2 D:THR93 4.5 47.2 1.0
CG2 C:THR199 4.6 37.3 1.0
CG2 C:THR93 4.6 43.5 1.0
CG2 D:THR199 4.7 45.4 1.0
N C:ILE200 4.7 39.0 1.0
N D:ILE94 4.8 34.1 1.0
N C:ILE94 4.8 34.8 1.0
N D:ILE200 4.8 42.4 1.0
O C:THR92 4.9 37.9 1.0
O C:THR198 4.9 42.2 1.0
O D:THR92 5.0 40.4 1.0

Reference:

K.E.J.Rodstrom, A.K.Kiper, W.Zhang, S.Rinne, A.C.W.Pike, M.Goldstein, L.Conrad, M.Delbeck, M.Hahn, H.Meier, M.Platzk, A.Quigley, D.Speedman, L.Shrestha, S.M.M.Mukhopadhyay, N.A.Burgess-Brown, S.J.Tucker, T.Mueller, N.Decher, E.P.Carpenter. A Unique Lower X-Gate in Task Channels Sequesters Inhibitors Within the Vestibule To Be Published.
Page generated: Mon Dec 14 01:27:42 2020

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