Potassium in PDB 2wlm: Potassium Channel From Magnetospirillum Magnetotacticum
Protein crystallography data
The structure of Potassium Channel From Magnetospirillum Magnetotacticum, PDB code: 2wlm
was solved by
O.B.Clarke,
A.T.Caputo,
B.J.Smith,
J.M.Gulbis,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
19.97 /
3.61
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
99.261,
151.193,
294.757,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
26.3 /
28.8
|
Potassium Binding Sites:
The binding sites of Potassium atom in the Potassium Channel From Magnetospirillum Magnetotacticum
(pdb code 2wlm). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the
Potassium Channel From Magnetospirillum Magnetotacticum, PDB code: 2wlm:
Jump to Potassium binding site number:
1;
2;
3;
4;
Potassium binding site 1 out
of 4 in 2wlm
Go back to
Potassium Binding Sites List in 2wlm
Potassium binding site 1 out
of 4 in the Potassium Channel From Magnetospirillum Magnetotacticum
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Potassium Channel From Magnetospirillum Magnetotacticum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K1296
b:0.5
occ:1.00
|
O
|
A:GLY98
|
3.0
|
0.3
|
1.0
|
O
|
C:GLY98
|
3.1
|
0.5
|
1.0
|
O
|
A:TYR99
|
3.1
|
0.9
|
1.0
|
O
|
C:TYR99
|
3.2
|
0.9
|
1.0
|
O
|
D:TYR99
|
3.2
|
0.0
|
1.0
|
O
|
B:GLY98
|
3.2
|
0.4
|
1.0
|
O
|
D:GLY98
|
3.2
|
0.8
|
1.0
|
O
|
B:TYR99
|
3.3
|
1.0
|
1.0
|
C
|
A:TYR99
|
3.9
|
0.2
|
1.0
|
C
|
C:TYR99
|
3.9
|
0.7
|
1.0
|
C
|
D:TYR99
|
4.0
|
0.9
|
1.0
|
C
|
B:TYR99
|
4.0
|
0.3
|
1.0
|
C
|
A:GLY98
|
4.2
|
0.9
|
1.0
|
C
|
C:GLY98
|
4.3
|
0.2
|
1.0
|
C
|
B:GLY98
|
4.4
|
0.5
|
1.0
|
C
|
D:GLY98
|
4.4
|
0.7
|
1.0
|
CA
|
A:TYR99
|
4.5
|
0.1
|
1.0
|
CA
|
C:TYR99
|
4.5
|
0.8
|
1.0
|
CA
|
D:TYR99
|
4.5
|
0.8
|
1.0
|
CA
|
B:TYR99
|
4.6
|
0.1
|
1.0
|
N
|
A:GLY100
|
4.7
|
0.4
|
1.0
|
N
|
C:GLY100
|
4.7
|
0.8
|
1.0
|
N
|
A:TYR99
|
4.8
|
0.6
|
1.0
|
N
|
C:TYR99
|
4.9
|
0.2
|
1.0
|
CA
|
C:GLY100
|
4.9
|
0.3
|
1.0
|
CA
|
A:GLY100
|
4.9
|
0.4
|
1.0
|
O
|
A:ILE97
|
4.9
|
0.6
|
1.0
|
N
|
B:GLY100
|
4.9
|
0.9
|
1.0
|
N
|
D:GLY100
|
4.9
|
0.7
|
1.0
|
O
|
D:ILE97
|
4.9
|
0.3
|
1.0
|
N
|
D:TYR99
|
4.9
|
0.7
|
1.0
|
O
|
C:ILE97
|
5.0
|
0.4
|
1.0
|
N
|
B:TYR99
|
5.0
|
0.5
|
1.0
|
O
|
B:ILE97
|
5.0
|
0.3
|
1.0
|
|
Potassium binding site 2 out
of 4 in 2wlm
Go back to
Potassium Binding Sites List in 2wlm
Potassium binding site 2 out
of 4 in the Potassium Channel From Magnetospirillum Magnetotacticum
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Potassium Channel From Magnetospirillum Magnetotacticum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K1297
b:0.3
occ:1.00
|
O
|
A:THR96
|
2.9
|
0.3
|
1.0
|
O
|
C:THR96
|
3.0
|
0.4
|
1.0
|
O
|
D:THR96
|
3.1
|
0.0
|
1.0
|
O
|
B:THR96
|
3.1
|
0.8
|
1.0
|
O
|
A:ILE97
|
3.1
|
0.6
|
1.0
|
O
|
C:ILE97
|
3.2
|
0.4
|
1.0
|
O
|
D:ILE97
|
3.2
|
0.3
|
1.0
|
O
|
B:ILE97
|
3.2
|
0.3
|
1.0
|
K
|
A:K1298
|
3.7
|
0.5
|
1.0
|
C
|
A:ILE97
|
3.7
|
0.5
|
1.0
|
C
|
C:ILE97
|
3.8
|
0.3
|
1.0
|
C
|
D:ILE97
|
3.8
|
0.6
|
1.0
|
C
|
B:ILE97
|
3.9
|
0.6
|
1.0
|
C
|
A:THR96
|
4.0
|
0.1
|
1.0
|
CA
|
A:ILE97
|
4.1
|
0.6
|
1.0
|
C
|
C:THR96
|
4.1
|
0.7
|
1.0
|
CA
|
D:ILE97
|
4.1
|
1.0
|
1.0
|
CA
|
C:ILE97
|
4.2
|
0.7
|
1.0
|
C
|
D:THR96
|
4.2
|
0.3
|
1.0
|
C
|
B:THR96
|
4.2
|
0.1
|
1.0
|
CA
|
B:ILE97
|
4.3
|
0.4
|
1.0
|
N
|
A:ILE97
|
4.6
|
0.2
|
1.0
|
N
|
A:GLY98
|
4.6
|
0.5
|
1.0
|
N
|
C:GLY98
|
4.6
|
0.8
|
1.0
|
N
|
C:ILE97
|
4.6
|
0.8
|
1.0
|
N
|
D:ILE97
|
4.7
|
0.7
|
1.0
|
N
|
D:GLY98
|
4.8
|
0.7
|
1.0
|
N
|
B:ILE97
|
4.8
|
0.2
|
1.0
|
N
|
B:GLY98
|
4.8
|
0.5
|
1.0
|
|
Potassium binding site 3 out
of 4 in 2wlm
Go back to
Potassium Binding Sites List in 2wlm
Potassium binding site 3 out
of 4 in the Potassium Channel From Magnetospirillum Magnetotacticum
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Potassium Channel From Magnetospirillum Magnetotacticum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K1298
b:0.5
occ:1.00
|
OG1
|
C:THR96
|
2.9
|
0.5
|
1.0
|
OG1
|
D:THR96
|
3.0
|
0.8
|
1.0
|
OG1
|
A:THR96
|
3.1
|
0.7
|
1.0
|
O
|
C:THR96
|
3.2
|
0.4
|
1.0
|
OG1
|
B:THR96
|
3.2
|
0.8
|
1.0
|
O
|
D:THR96
|
3.3
|
0.0
|
1.0
|
O
|
A:THR96
|
3.3
|
0.3
|
1.0
|
O
|
B:THR96
|
3.5
|
0.8
|
1.0
|
K
|
A:K1297
|
3.7
|
0.3
|
1.0
|
CB
|
C:THR96
|
3.9
|
0.4
|
1.0
|
CB
|
A:THR96
|
4.1
|
1.0
|
1.0
|
CB
|
D:THR96
|
4.1
|
1.0
|
1.0
|
C
|
C:THR96
|
4.1
|
0.7
|
1.0
|
C
|
D:THR96
|
4.2
|
0.3
|
1.0
|
C
|
A:THR96
|
4.2
|
0.1
|
1.0
|
CB
|
B:THR96
|
4.2
|
0.7
|
1.0
|
C
|
B:THR96
|
4.4
|
0.1
|
1.0
|
O
|
D:ALA95
|
4.5
|
0.5
|
1.0
|
O
|
A:ALA95
|
4.6
|
0.3
|
1.0
|
O
|
C:ALA95
|
4.6
|
0.5
|
1.0
|
CA
|
C:THR96
|
4.7
|
0.8
|
1.0
|
CA
|
A:THR96
|
4.8
|
1.0
|
1.0
|
CA
|
D:THR96
|
4.8
|
0.3
|
1.0
|
O
|
B:ALA95
|
4.9
|
1.0
|
1.0
|
|
Potassium binding site 4 out
of 4 in 2wlm
Go back to
Potassium Binding Sites List in 2wlm
Potassium binding site 4 out
of 4 in the Potassium Channel From Magnetospirillum Magnetotacticum
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of Potassium Channel From Magnetospirillum Magnetotacticum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K1299
b:98.2
occ:1.00
|
OH
|
B:TYR132
|
3.8
|
91.7
|
1.0
|
OH
|
C:TYR132
|
3.9
|
77.6
|
1.0
|
OH
|
A:TYR132
|
4.5
|
98.1
|
1.0
|
CZ
|
B:TYR132
|
4.6
|
90.8
|
1.0
|
CE2
|
B:TYR132
|
4.7
|
89.5
|
1.0
|
OH
|
D:TYR132
|
4.8
|
68.4
|
1.0
|
CZ
|
C:TYR132
|
4.9
|
84.5
|
1.0
|
|
Reference:
O.B.Clarke,
A.T.Caputo,
A.P.Hill,
J.I.Vandenberg,
B.J.Smith,
J.M.Gulbis.
Domain Reorientation and Rotation of An Intracellular Assembly Regulate Conduction in Kir Potassium Channels. Cell(Cambridge,Mass.) V. 141 1018 2010.
ISSN: ISSN 0092-8674
PubMed: 20564790
DOI: 10.1016/J.CELL.2010.05.003
Page generated: Mon Aug 12 07:32:12 2024
|