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Potassium in PDB 6w88: K2P2.1 (Trek-1):ML335 Complex, 30 Mm K+

Protein crystallography data

The structure of K2P2.1 (Trek-1):ML335 Complex, 30 Mm K+, PDB code: 6w88 was solved by M.Lolicato, D.L.Minor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.99 / 3.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 67.006, 119.996, 128.794, 90, 90, 90
R / Rfree (%) 25.9 / 29.4

Other elements in 6w88:

The structure of K2P2.1 (Trek-1):ML335 Complex, 30 Mm K+ also contains other interesting chemical elements:

Cadmium (Cd) 4 atoms
Chlorine (Cl) 4 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the K2P2.1 (Trek-1):ML335 Complex, 30 Mm K+ (pdb code 6w88). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 5 binding sites of Potassium where determined in the K2P2.1 (Trek-1):ML335 Complex, 30 Mm K+, PDB code: 6w88:
Jump to Potassium binding site number: 1; 2; 3; 4; 5;

Potassium binding site 1 out of 5 in 6w88

Go back to Potassium Binding Sites List in 6w88
Potassium binding site 1 out of 5 in the K2P2.1 (Trek-1):ML335 Complex, 30 Mm K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of K2P2.1 (Trek-1):ML335 Complex, 30 Mm K+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K409

b:190.4
occ:1.00
 CD1 A:LEU289 4.6 93.0 1.0
CG2 B:ILE167 4.9 122.1 1.0
O A:THR250 5.0 105.3 1.0

Potassium binding site 2 out of 5 in 6w88

Go back to Potassium Binding Sites List in 6w88
Potassium binding site 2 out of 5 in the K2P2.1 (Trek-1):ML335 Complex, 30 Mm K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of K2P2.1 (Trek-1):ML335 Complex, 30 Mm K+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K410

b:143.7
occ:1.00
 O B:PHE254 2.7 115.6 1.0
O A:PHE145 2.8 112.2 1.0
O A:PHE254 2.8 121.7 1.0
O B:PHE145 2.8 138.8 1.0
O B:GLY253 3.2 121.6 1.0
O A:GLY144 3.2 113.9 1.0
O B:GLY144 3.2 122.2 1.0
O A:GLY253 3.3 110.7 1.0
C B:PHE254 3.5 116.7 1.0
C A:PHE145 3.6 113.4 1.0
K B:K412 3.6 134.3 1.0
C A:PHE254 3.6 119.6 1.0
C B:PHE145 3.7 138.8 1.0
CA B:PHE254 4.0 111.5 1.0
CA A:PHE254 4.2 116.2 1.0
CA A:PHE145 4.2 108.6 1.0
C B:GLY253 4.2 117.8 1.0
CA B:PHE145 4.3 134.0 1.0
C A:GLY144 4.3 112.9 1.0
C A:GLY253 4.3 107.8 1.0
C B:GLY144 4.4 123.6 1.0
N A:GLY146 4.4 116.5 1.0
N B:GLY255 4.5 120.0 1.0
N B:GLY146 4.5 142.2 1.0
CA A:GLY146 4.5 120.2 1.0
N B:PHE254 4.6 114.2 1.0
N A:GLY255 4.6 120.4 1.0
CA B:GLY146 4.7 146.8 1.0
N A:PHE254 4.7 112.0 1.0
N A:PHE145 4.8 111.7 1.0
N B:PHE145 4.9 128.8 1.0
CA A:GLY255 5.0 124.2 1.0
CA B:GLY255 5.0 123.3 1.0

Potassium binding site 3 out of 5 in 6w88

Go back to Potassium Binding Sites List in 6w88
Potassium binding site 3 out of 5 in the K2P2.1 (Trek-1):ML335 Complex, 30 Mm K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of K2P2.1 (Trek-1):ML335 Complex, 30 Mm K+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K411

b:135.4
occ:1.00
 K B:K412 2.8 134.3 1.0
O B:THR251 2.8 109.2 1.0
O A:THR251 2.8 101.1 1.0
O A:ILE252 2.8 102.9 1.0
O B:ILE252 2.9 119.9 1.0
O B:THR142 3.0 107.7 1.0
O B:ILE143 3.0 116.2 1.0
O A:THR142 3.0 112.9 1.0
O A:ILE143 3.1 109.9 1.0
K A:K412 3.6 97.2 1.0
C A:ILE252 3.7 98.8 1.0
C B:ILE252 3.7 117.5 1.0
C B:ILE143 3.7 117.8 1.0
C A:ILE143 3.8 111.5 1.0
C B:THR251 3.9 109.5 1.0
C A:THR251 3.9 100.3 1.0
C B:THR142 4.0 106.5 1.0
C A:THR142 4.0 112.0 1.0
CA A:ILE252 4.2 98.3 1.0
CA B:ILE143 4.3 118.7 1.0
CA B:ILE252 4.3 115.6 1.0
CA A:ILE143 4.3 110.6 1.0
N B:ILE252 4.6 112.4 1.0
N A:ILE252 4.6 98.5 1.0
N B:GLY144 4.6 118.1 1.0
N A:GLY253 4.6 96.9 1.0
N B:ILE143 4.6 112.2 1.0
N B:GLY253 4.6 118.0 1.0
N A:GLY144 4.6 112.7 1.0
N A:ILE143 4.7 111.2 1.0
CA A:GLY253 4.8 99.6 1.0
O A:GLY144 4.8 113.9 1.0
O B:GLY144 4.8 122.2 1.0
O A:GLY253 4.8 110.7 1.0
CA B:GLY253 4.8 118.8 1.0
O B:GLY253 4.9 121.6 1.0
CA B:GLY144 4.9 120.5 1.0
CA A:GLY144 4.9 113.5 1.0
CA B:THR251 5.0 106.4 1.0
CA B:THR142 5.0 99.1 1.0

Potassium binding site 4 out of 5 in 6w88

Go back to Potassium Binding Sites List in 6w88
Potassium binding site 4 out of 5 in the K2P2.1 (Trek-1):ML335 Complex, 30 Mm K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of K2P2.1 (Trek-1):ML335 Complex, 30 Mm K+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K412

b:97.2
occ:1.00
 O B:THR142 2.8 107.7 1.0
OG1 A:THR251 2.9 109.2 1.0
O A:THR251 2.9 101.1 1.0
O A:THR142 3.0 112.9 1.0
OG1 B:THR142 3.0 91.1 1.0
OG1 B:THR251 3.0 112.2 1.0
O B:THR251 3.1 109.2 1.0
OG1 A:THR142 3.3 120.9 1.0
CB A:THR251 3.5 106.0 1.0
CB B:THR251 3.6 108.4 1.0
K A:K411 3.6 135.4 1.0
CB B:THR142 3.6 93.8 1.0
C A:THR251 3.8 100.3 1.0
C B:THR142 3.9 106.5 1.0
CB A:THR142 3.9 117.5 1.0
C A:THR142 4.0 112.0 1.0
C B:THR251 4.1 109.5 1.0
CA A:THR251 4.3 102.0 1.0
CA B:THR142 4.4 99.1 1.0
CA B:THR251 4.5 106.4 1.0
CA A:THR142 4.6 112.1 1.0
CG2 A:THR251 4.7 105.3 1.0
CG2 B:THR251 4.7 107.3 1.0
N A:ILE252 4.8 98.5 1.0
O A:THR250 4.8 105.3 1.0
CG2 B:THR142 4.9 91.5 1.0
O B:THR141 5.0 100.3 1.0
N B:ILE143 5.0 112.2 1.0

Potassium binding site 5 out of 5 in 6w88

Go back to Potassium Binding Sites List in 6w88
Potassium binding site 5 out of 5 in the K2P2.1 (Trek-1):ML335 Complex, 30 Mm K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 5 of K2P2.1 (Trek-1):ML335 Complex, 30 Mm K+ within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K412

b:134.3
occ:1.00
 O B:GLY253 2.7 121.6 1.0
O B:ILE252 2.7 119.9 1.0
K A:K411 2.8 135.4 1.0
O A:GLY144 2.8 113.9 1.0
O B:GLY144 2.8 122.2 1.0
O B:ILE143 2.9 116.2 1.0
O A:GLY253 2.9 110.7 1.0
O A:ILE252 3.0 102.9 1.0
O A:ILE143 3.0 109.9 1.0
C B:GLY253 3.4 117.8 1.0
K A:K410 3.6 143.7 1.0
C A:GLY144 3.7 112.9 1.0
C B:GLY144 3.7 123.6 1.0
C A:GLY253 3.7 107.8 1.0
C B:ILE252 3.9 117.5 1.0
CA B:GLY253 4.0 118.8 1.0
C B:ILE143 4.0 117.8 1.0
C A:ILE143 4.1 111.5 1.0
CA A:GLY144 4.1 113.5 1.0
C A:ILE252 4.2 98.8 1.0
CA B:GLY144 4.2 120.5 1.0
CA A:GLY253 4.3 99.6 1.0
N B:PHE254 4.3 114.2 1.0
N B:GLY253 4.4 118.0 1.0
N B:GLY144 4.6 118.1 1.0
N A:PHE254 4.6 112.0 1.0
N A:GLY144 4.6 112.7 1.0
N B:PHE145 4.7 128.8 1.0
N A:GLY253 4.7 96.9 1.0
N A:PHE145 4.7 111.7 1.0
CA B:PHE254 4.8 111.5 1.0
O B:THR251 4.8 109.2 1.0
O A:THR251 5.0 101.1 1.0

Reference:

M.Lolicato, A.M.Natale, F.Abderemane-Ali, D.Crottes, S.Capponi, R.Duman, A.Wagner, J.M.Rosenberg, M.Grabe, D.L.Minor Jr.. K 2P Channel C-Type Gating Involves Asymmetric Selectivity Filter Order-Disorder Transitions. Sci Adv V. 6 2020.
ISSN: ESSN 2375-2548
PubMed: 33127683
DOI: 10.1126/SCIADV.ABC9174
Page generated: Mon Aug 12 18:09:50 2024

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