Bromine in PDB 6rv3: Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation with A Bound Inhibitor Bay 1000493

The structure of Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation with A Bound Inhibitor Bay 1000493, PDB code: 6rv3 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)	41.31 / 2.90
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.070, 204.500, 239.320, 90.00, 90.00, 90.00
R / Rfree (%)	23.5 / 24.2

The structure of Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation with A Bound Inhibitor Bay 1000493 also contains other interesting chemical elements:

Fluorine	(F)	4 atoms
Potassium	(K)	8 atoms

The binding sites of Bromine atom in the Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation with A Bound Inhibitor Bay 1000493 (pdb code 6rv3). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 4 binding sites of Bromine where determined in the Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation with A Bound Inhibitor Bay 1000493, PDB code: 6rv3:
Jump to Bromine binding site number: 1; 2; 3; 4;

Bromine binding site 1 out of 4 in the Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation with A Bound Inhibitor Bay 1000493


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation with A Bound Inhibitor Bay 1000493 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br300 b:42.2 occ:0.50 BR1 A:KKQ300 0.0 42.2 0.5 C16 A:KKQ300 1.9 41.0 0.5 C15 A:KKQ300 2.8 40.8 0.5 C17 A:KKQ300 2.9 40.6 0.5 CG2 B:ILE118 3.8 26.4 1.0 CD2 A:LEU239 4.1 40.2 1.0 C14 A:KKQ300 4.1 41.2 0.5 C18 A:KKQ300 4.2 41.0 0.5 CG2 A:THR198 4.2 28.0 1.0 CB B:ILE118 4.3 26.4 1.0 CG2 A:ILE235 4.4 35.0 1.0 CD1 B:ILE118 4.5 33.9 1.0 CB A:THR198 4.7 26.0 1.0 C13 A:KKQ300 4.7 42.4 0.5 C22 A:KKQ300 4.8 52.5 0.5 CA A:THR198 4.8 17.2 1.0 CG A:LEU239 4.8 38.3 1.0 CD1 A:LEU239 4.9 38.2 1.0 CD B:PRO119 4.9 27.5 1.0 CG B:PRO119 5.0 32.0 1.0

Bromine binding site 2 out of 4 in the Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation with A Bound Inhibitor Bay 1000493


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation with A Bound Inhibitor Bay 1000493 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br300 b:50.3 occ:0.50 BR1 A:KKQ300 0.0 50.3 0.5 C16 A:KKQ300 1.9 47.2 0.5 C15 A:KKQ300 2.8 46.1 0.5 C17 A:KKQ300 2.9 45.8 0.5 CG2 A:ILE118 3.8 28.8 1.0 CD2 B:LEU239 3.9 35.3 1.0 C14 A:KKQ300 4.1 46.0 0.5 CB A:ILE118 4.2 28.9 1.0 C18 A:KKQ300 4.2 45.5 0.5 CG2 B:THR198 4.3 18.9 1.0 CD1 B:LEU239 4.3 34.9 1.0 CD1 A:ILE118 4.5 30.1 1.0 C22 A:KKQ300 4.5 43.3 0.5 CG2 B:ILE235 4.5 34.8 1.0 CG B:LEU239 4.6 34.8 1.0 CG A:PRO119 4.7 32.9 1.0 C13 A:KKQ300 4.7 46.5 0.5 CB B:THR198 4.7 23.7 1.0 CD A:PRO119 4.7 28.6 1.0 CA B:THR198 4.9 15.9 1.0 CG1 A:ILE118 4.9 28.5 1.0

Bromine binding site 3 out of 4 in the Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation with A Bound Inhibitor Bay 1000493


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation with A Bound Inhibitor Bay 1000493 within 5.0Å range: probe atom residue distance (Å) B Occ C:Br306 b:65.1 occ:0.50 BR1 C:KKQ306 0.0 65.1 0.5 C16 C:KKQ306 1.9 64.8 0.5 C15 C:KKQ306 2.8 65.2 0.5 C17 C:KKQ306 2.9 64.7 0.5 CG2 D:ILE118 3.9 32.3 1.0 CD2 C:LEU239 4.0 45.2 1.0 C14 C:KKQ306 4.1 65.9 0.5 C18 C:KKQ306 4.2 65.1 0.5 CG2 C:THR198 4.3 24.7 1.0 CG2 C:ILE235 4.3 45.5 1.0 CB D:ILE118 4.4 31.4 1.0 CD1 D:ILE118 4.6 38.0 1.0 CB C:THR198 4.7 25.9 1.0 C13 C:KKQ306 4.7 66.2 0.5 C22 C:KKQ306 4.8 63.9 0.5 CA C:THR198 4.9 15.7 1.0 CG C:LEU239 4.9 43.1 1.0 CD1 C:LEU239 5.0 43.0 1.0 CD D:PRO119 5.0 32.5 1.0

Bromine binding site 4 out of 4 in the Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation with A Bound Inhibitor Bay 1000493


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Crystal Structure of the Human Two Pore Domain Potassium Ion Channel Task-1 (K2P3.1) in A Closed Conformation with A Bound Inhibitor Bay 1000493 within 5.0Å range: probe atom residue distance (Å) B Occ C:Br306 b:62.1 occ:0.50 BR1 C:KKQ306 0.0 62.1 0.5 C16 C:KKQ306 1.9 61.1 0.5 C15 C:KKQ306 2.8 60.8 0.5 C17 C:KKQ306 2.9 60.3 0.5 CD2 D:LEU239 3.8 47.3 1.0 CG2 C:ILE118 3.8 35.6 1.0 C14 C:KKQ306 4.1 60.5 0.5 C18 C:KKQ306 4.2 59.8 0.5 CB C:ILE118 4.2 34.7 1.0 CG2 D:THR198 4.3 33.0 1.0 CG2 D:ILE235 4.4 35.8 1.0 CD1 C:ILE118 4.5 41.2 1.0 C22 C:KKQ306 4.5 76.8 0.5 C13 C:KKQ306 4.7 60.0 0.5 CB D:THR198 4.7 33.6 1.0 CD C:PRO119 4.8 37.2 1.0 CG D:LEU239 4.8 45.0 1.0 CD1 D:LEU239 4.9 45.2 1.0 CG C:PRO119 4.9 41.8 1.0 CA D:THR198 4.9 27.5 1.0 CG1 C:ILE118 5.0 35.1 1.0

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.