Potassium in PDB 8vc3: Voltage Gated Potassium Ion Channel KV1.2 in Complex with Dtx
Potassium Binding Sites:
The binding sites of Potassium atom in the Voltage Gated Potassium Ion Channel KV1.2 in Complex with Dtx
(pdb code 8vc3). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the
Voltage Gated Potassium Ion Channel KV1.2 in Complex with Dtx, PDB code: 8vc3:
Jump to Potassium binding site number:
1;
2;
Potassium binding site 1 out
of 2 in 8vc3
Go back to
Potassium Binding Sites List in 8vc3
Potassium binding site 1 out
of 2 in the Voltage Gated Potassium Ion Channel KV1.2 in Complex with Dtx
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Voltage Gated Potassium Ion Channel KV1.2 in Complex with Dtx within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K101
b:9.8
occ:1.00
|
O
|
E:GLY376
|
2.5
|
12.0
|
1.0
|
O
|
B:GLY376
|
2.5
|
9.3
|
1.0
|
O
|
D:GLY376
|
2.5
|
10.3
|
1.0
|
O
|
C:GLY376
|
2.5
|
10.1
|
1.0
|
NZ
|
A:LYS5
|
2.5
|
14.4
|
1.0
|
C
|
D:GLY376
|
3.7
|
8.2
|
1.0
|
C
|
E:GLY376
|
3.7
|
9.3
|
1.0
|
C
|
B:GLY376
|
3.7
|
8.1
|
1.0
|
C
|
C:GLY376
|
3.7
|
7.4
|
1.0
|
O
|
E:TYR377
|
3.9
|
18.0
|
1.0
|
O
|
B:TYR377
|
3.9
|
14.9
|
1.0
|
O
|
D:TYR377
|
3.9
|
14.9
|
1.0
|
C
|
D:TYR377
|
3.9
|
12.8
|
1.0
|
O
|
C:TYR377
|
4.0
|
14.2
|
1.0
|
CE
|
A:LYS5
|
4.0
|
20.4
|
1.0
|
C
|
C:TYR377
|
4.1
|
10.6
|
1.0
|
CA
|
D:TYR377
|
4.1
|
9.3
|
1.0
|
C
|
E:TYR377
|
4.1
|
15.5
|
1.0
|
C
|
B:TYR377
|
4.1
|
15.5
|
1.0
|
CA
|
E:TYR377
|
4.2
|
12.1
|
1.0
|
O
|
D:VAL375
|
4.3
|
9.7
|
1.0
|
N
|
D:TYR377
|
4.4
|
10.4
|
1.0
|
O
|
C:VAL375
|
4.4
|
10.6
|
1.0
|
CA
|
C:TYR377
|
4.4
|
8.6
|
1.0
|
N
|
E:TYR377
|
4.4
|
11.7
|
1.0
|
CA
|
B:TYR377
|
4.4
|
13.8
|
1.0
|
O
|
E:VAL375
|
4.5
|
9.9
|
1.0
|
N
|
D:GLY378
|
4.5
|
12.3
|
1.0
|
N
|
B:TYR377
|
4.6
|
11.8
|
1.0
|
N
|
C:GLY378
|
4.6
|
10.0
|
1.0
|
N
|
C:TYR377
|
4.6
|
9.1
|
1.0
|
O
|
B:VAL375
|
4.6
|
10.6
|
1.0
|
CA
|
B:GLY376
|
4.7
|
6.0
|
1.0
|
CA
|
C:GLY376
|
4.7
|
5.0
|
1.0
|
CD
|
A:LYS5
|
4.7
|
22.6
|
1.0
|
CA
|
E:GLY376
|
4.8
|
6.7
|
1.0
|
N
|
B:GLY378
|
4.8
|
14.1
|
1.0
|
CA
|
D:GLY376
|
4.8
|
5.7
|
1.0
|
N
|
E:GLY378
|
4.9
|
13.8
|
1.0
|
CA
|
C:GLY378
|
4.9
|
9.5
|
1.0
|
|
Potassium binding site 2 out
of 2 in 8vc3
Go back to
Potassium Binding Sites List in 8vc3
Potassium binding site 2 out
of 2 in the Voltage Gated Potassium Ion Channel KV1.2 in Complex with Dtx
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Voltage Gated Potassium Ion Channel KV1.2 in Complex with Dtx within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K501
b:1.6
occ:1.00
|
O
|
B:VAL375
|
2.7
|
10.6
|
1.0
|
O
|
D:THR374
|
2.7
|
5.5
|
1.0
|
O
|
E:THR374
|
2.8
|
7.8
|
1.0
|
O
|
C:THR374
|
2.8
|
9.8
|
1.0
|
O
|
E:VAL375
|
2.9
|
9.9
|
1.0
|
O
|
B:THR374
|
2.9
|
7.2
|
1.0
|
O
|
C:VAL375
|
3.0
|
10.6
|
1.0
|
O
|
D:VAL375
|
3.1
|
9.7
|
1.0
|
C
|
B:VAL375
|
3.4
|
9.1
|
1.0
|
C
|
E:VAL375
|
3.5
|
8.0
|
1.0
|
C
|
C:VAL375
|
3.7
|
8.4
|
1.0
|
C
|
D:VAL375
|
3.7
|
8.2
|
1.0
|
C
|
D:THR374
|
3.8
|
5.7
|
1.0
|
C
|
B:THR374
|
3.8
|
6.3
|
1.0
|
C
|
E:THR374
|
3.9
|
7.4
|
1.0
|
CA
|
B:VAL375
|
3.9
|
6.2
|
1.0
|
C
|
C:THR374
|
3.9
|
7.9
|
1.0
|
CA
|
E:VAL375
|
4.0
|
6.3
|
1.0
|
CA
|
C:VAL375
|
4.0
|
6.3
|
1.0
|
CA
|
D:VAL375
|
4.1
|
6.0
|
1.0
|
N
|
B:VAL375
|
4.3
|
6.1
|
1.0
|
N
|
B:GLY376
|
4.3
|
7.9
|
1.0
|
N
|
E:GLY376
|
4.3
|
7.6
|
1.0
|
N
|
E:VAL375
|
4.4
|
6.8
|
1.0
|
N
|
D:VAL375
|
4.4
|
6.0
|
1.0
|
N
|
C:VAL375
|
4.5
|
7.5
|
1.0
|
N
|
C:GLY376
|
4.6
|
6.5
|
1.0
|
CA
|
E:GLY376
|
4.7
|
6.7
|
1.0
|
CA
|
B:GLY376
|
4.7
|
6.0
|
1.0
|
N
|
D:GLY376
|
4.7
|
6.7
|
1.0
|
O
|
B:GLY376
|
4.9
|
9.3
|
1.0
|
CA
|
D:THR374
|
4.9
|
6.7
|
1.0
|
O
|
E:GLY376
|
4.9
|
12.0
|
1.0
|
CA
|
B:THR374
|
5.0
|
6.6
|
1.0
|
|
Reference:
Y.Wu,
Y.Yan,
Y.Yang,
S.Bian,
A.Rivetta,
K.Allen,
F.J.Sigworth.
Cryo-Em Structures of KV1.2 Potassium Channels, Conducting and Non-Conducting. Biorxiv 2023.
ISSN: ISSN 2692-8205
PubMed: 37398110
DOI: 10.1101/2023.06.02.543446
Page generated: Sat Aug 9 18:09:46 2025
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