Potassium in PDB 7n9k: KIRBAC3.1 L124M Mutant
Protein crystallography data
The structure of KIRBAC3.1 L124M Mutant, PDB code: 7n9k
was solved by
T.A.Black,
J.M.Gulbis,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
42.08 /
2.72
|
Space group
|
P 4 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
106.577,
106.577,
89.597,
90,
90,
90
|
R / Rfree (%)
|
21.8 /
25
|
Potassium Binding Sites:
The binding sites of Potassium atom in the KIRBAC3.1 L124M Mutant
(pdb code 7n9k). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 7 binding sites of Potassium where determined in the
KIRBAC3.1 L124M Mutant, PDB code: 7n9k:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
7;
Potassium binding site 1 out
of 7 in 7n9k
Go back to
Potassium Binding Sites List in 7n9k
Potassium binding site 1 out
of 7 in the KIRBAC3.1 L124M Mutant
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of KIRBAC3.1 L124M Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K506
b:59.1
occ:0.18
|
O
|
A:GLY98
|
2.7
|
53.4
|
1.0
|
O
|
A:TYR99
|
2.8
|
59.1
|
1.0
|
C
|
A:TYR99
|
3.6
|
57.6
|
1.0
|
C
|
A:GLY98
|
3.9
|
49.9
|
1.0
|
HA
|
A:TYR99
|
4.0
|
76.7
|
1.0
|
CA
|
A:TYR99
|
4.3
|
63.7
|
1.0
|
HA2
|
A:GLY100
|
4.3
|
95.5
|
1.0
|
HA3
|
A:GLY100
|
4.3
|
95.5
|
1.0
|
N
|
A:GLY100
|
4.4
|
66.9
|
1.0
|
N
|
A:TYR99
|
4.6
|
55.7
|
1.0
|
CA
|
A:GLY100
|
4.6
|
79.4
|
1.0
|
HA3
|
A:GLY98
|
4.8
|
60.6
|
1.0
|
|
Potassium binding site 2 out
of 7 in 7n9k
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Potassium Binding Sites List in 7n9k
Potassium binding site 2 out
of 7 in the KIRBAC3.1 L124M Mutant
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of KIRBAC3.1 L124M Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K507
b:57.6
occ:0.14
|
O
|
A:THR96
|
2.7
|
55.1
|
1.0
|
O
|
A:ILE97
|
2.8
|
57.4
|
1.0
|
K
|
A:K508
|
3.4
|
57.2
|
0.2
|
HA
|
A:ILE97
|
3.5
|
65.9
|
1.0
|
C
|
A:ILE97
|
3.5
|
54.6
|
1.0
|
C
|
A:THR96
|
3.8
|
52.3
|
1.0
|
CA
|
A:ILE97
|
4.0
|
54.7
|
1.0
|
HA3
|
A:GLY98
|
4.4
|
60.6
|
1.0
|
N
|
A:ILE97
|
4.4
|
53.5
|
1.0
|
N
|
A:GLY98
|
4.5
|
48.1
|
1.0
|
HB
|
A:THR96
|
4.6
|
70.0
|
1.0
|
HG1
|
A:THR96
|
4.6
|
74.0
|
1.0
|
CA
|
A:GLY98
|
4.9
|
50.3
|
1.0
|
|
Potassium binding site 3 out
of 7 in 7n9k
Go back to
Potassium Binding Sites List in 7n9k
Potassium binding site 3 out
of 7 in the KIRBAC3.1 L124M Mutant
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of KIRBAC3.1 L124M Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K508
b:57.2
occ:0.18
|
HG1
|
A:THR96
|
2.4
|
74.0
|
1.0
|
O
|
A:THR96
|
2.9
|
55.1
|
1.0
|
OG1
|
A:THR96
|
2.9
|
61.5
|
1.0
|
HB
|
A:THR96
|
3.2
|
70.0
|
1.0
|
K
|
A:K507
|
3.4
|
57.6
|
0.1
|
CB
|
A:THR96
|
3.6
|
58.1
|
1.0
|
C
|
A:THR96
|
3.8
|
52.3
|
1.0
|
CA
|
A:THR96
|
4.4
|
51.2
|
1.0
|
K
|
A:K509
|
4.4
|
107.5
|
0.2
|
HA
|
A:ILE97
|
4.5
|
65.9
|
1.0
|
O
|
A:ALA95
|
4.6
|
54.8
|
1.0
|
HG21
|
A:THR96
|
4.8
|
57.0
|
1.0
|
CG2
|
A:THR96
|
4.8
|
47.3
|
1.0
|
N
|
A:ILE97
|
4.8
|
53.5
|
1.0
|
HA
|
A:THR96
|
5.0
|
61.7
|
1.0
|
|
Potassium binding site 4 out
of 7 in 7n9k
Go back to
Potassium Binding Sites List in 7n9k
Potassium binding site 4 out
of 7 in the KIRBAC3.1 L124M Mutant
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of KIRBAC3.1 L124M Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K509
b:107.5
occ:0.25
|
K
|
A:K511
|
3.2
|
85.1
|
0.7
|
OG1
|
A:THR96
|
4.3
|
61.5
|
1.0
|
K
|
A:K508
|
4.4
|
57.2
|
0.2
|
HG1
|
A:THR96
|
4.5
|
74.0
|
1.0
|
H41
|
A:OCT505
|
4.5
|
78.0
|
1.0
|
H42
|
A:OCT505
|
4.6
|
78.0
|
1.0
|
|
Potassium binding site 5 out
of 7 in 7n9k
Go back to
Potassium Binding Sites List in 7n9k
Potassium binding site 5 out
of 7 in the KIRBAC3.1 L124M Mutant
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 5 of KIRBAC3.1 L124M Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K510
b:68.4
occ:0.25
|
K
|
A:K512
|
4.2
|
81.2
|
0.8
|
CG
|
A:TYR132
|
4.7
|
39.6
|
1.0
|
CD1
|
A:TYR132
|
4.7
|
41.3
|
1.0
|
CD2
|
A:TYR132
|
4.8
|
38.2
|
1.0
|
CE1
|
A:TYR132
|
4.9
|
32.8
|
1.0
|
HB2
|
A:TYR132
|
4.9
|
39.6
|
1.0
|
CE2
|
A:TYR132
|
4.9
|
32.2
|
1.0
|
CZ
|
A:TYR132
|
5.0
|
35.7
|
1.0
|
HD1
|
A:TYR132
|
5.0
|
49.8
|
1.0
|
|
Potassium binding site 6 out
of 7 in 7n9k
Go back to
Potassium Binding Sites List in 7n9k
Potassium binding site 6 out
of 7 in the KIRBAC3.1 L124M Mutant
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 6 of KIRBAC3.1 L124M Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K511
b:85.1
occ:0.68
|
K
|
A:K509
|
3.2
|
107.5
|
0.2
|
HG21
|
A:THR96
|
3.6
|
57.0
|
1.0
|
SD
|
A:MET124
|
3.7
|
76.9
|
1.0
|
HG23
|
A:THR96
|
3.8
|
57.0
|
1.0
|
HE1
|
A:MET124
|
3.9
|
92.3
|
1.0
|
OG1
|
A:THR96
|
4.0
|
61.5
|
1.0
|
CG2
|
A:THR96
|
4.1
|
47.3
|
1.0
|
CE
|
A:MET124
|
4.4
|
76.7
|
1.0
|
H42
|
A:OCT505
|
4.4
|
78.0
|
1.0
|
H31
|
A:OCT505
|
4.5
|
70.9
|
1.0
|
O
|
A:ALA95
|
4.5
|
54.8
|
1.0
|
H32
|
A:OCT505
|
4.5
|
70.9
|
1.0
|
HG2
|
A:MET121
|
4.6
|
78.1
|
0.5
|
HG1
|
A:THR96
|
4.6
|
74.0
|
1.0
|
CB
|
A:THR96
|
4.7
|
58.1
|
1.0
|
HG3
|
A:MET121
|
4.7
|
78.1
|
0.5
|
H41
|
A:OCT505
|
4.8
|
78.0
|
1.0
|
HE2
|
A:MET121
|
4.8
|
69.7
|
0.5
|
C3
|
A:OCT505
|
4.9
|
58.9
|
1.0
|
C4
|
A:OCT505
|
4.9
|
64.8
|
1.0
|
HE2
|
A:MET124
|
5.0
|
92.3
|
1.0
|
HG22
|
A:THR96
|
5.0
|
57.0
|
1.0
|
|
Potassium binding site 7 out
of 7 in 7n9k
Go back to
Potassium Binding Sites List in 7n9k
Potassium binding site 7 out
of 7 in the KIRBAC3.1 L124M Mutant
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 7 of KIRBAC3.1 L124M Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K512
b:81.2
occ:0.85
|
H82
|
A:OCT505
|
2.8
|
61.0
|
1.0
|
HB1
|
A:ALA128
|
3.2
|
47.3
|
1.0
|
H81
|
A:OCT505
|
3.3
|
61.0
|
1.0
|
C8
|
A:OCT505
|
3.3
|
50.6
|
1.0
|
HB2
|
A:TYR132
|
3.9
|
39.6
|
1.0
|
CB
|
A:ALA128
|
4.2
|
39.2
|
1.0
|
K
|
A:K510
|
4.2
|
68.4
|
0.2
|
HB3
|
A:ALA128
|
4.4
|
47.3
|
1.0
|
O
|
A:ALA128
|
4.6
|
47.5
|
1.0
|
HB2
|
A:ALA128
|
4.7
|
47.3
|
1.0
|
C7
|
A:OCT505
|
4.7
|
46.7
|
1.0
|
HD1
|
A:TYR132
|
4.7
|
49.8
|
1.0
|
C
|
A:ALA128
|
4.8
|
44.3
|
1.0
|
CB
|
A:TYR132
|
4.8
|
32.8
|
1.0
|
H71
|
A:OCT505
|
4.9
|
56.2
|
1.0
|
HB3
|
A:TYR132
|
5.0
|
39.6
|
1.0
|
CA
|
A:ALA128
|
5.0
|
40.4
|
1.0
|
|
Reference:
J.M.Gulbis,
K.A.Black.
Ion Currents Through Kir Potassium Channels Are Gated By Anionic Lipids. Nat Commun 2021.
ISSN: ESSN 2041-1723
Page generated: Mon Aug 12 19:28:58 2024
|