Potassium in PDB 6ys9: T_926 Truncate of Chlh From Thermosynechococcus Elongatus at 1.64 A Resolution
Protein crystallography data
The structure of T_926 Truncate of Chlh From Thermosynechococcus Elongatus at 1.64 A Resolution, PDB code: 6ys9
was solved by
C.Bisson,
C.N.Hunter,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
64.38 /
1.64
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
76.480,
140.330,
78.010,
90.00,
108.66,
90.00
|
R / Rfree (%)
|
20.1 /
24.7
|
Potassium Binding Sites:
The binding sites of Potassium atom in the T_926 Truncate of Chlh From Thermosynechococcus Elongatus at 1.64 A Resolution
(pdb code 6ys9). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the
T_926 Truncate of Chlh From Thermosynechococcus Elongatus at 1.64 A Resolution, PDB code: 6ys9:
Jump to Potassium binding site number:
1;
2;
3;
4;
Potassium binding site 1 out
of 4 in 6ys9
Go back to
Potassium Binding Sites List in 6ys9
Potassium binding site 1 out
of 4 in the T_926 Truncate of Chlh From Thermosynechococcus Elongatus at 1.64 A Resolution
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of T_926 Truncate of Chlh From Thermosynechococcus Elongatus at 1.64 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K501
b:35.4
occ:1.00
|
O
|
A:HOH680
|
2.8
|
31.0
|
1.0
|
N
|
A:GLY111
|
3.3
|
19.7
|
1.0
|
N
|
A:ALA174
|
3.3
|
15.7
|
1.0
|
O
|
A:HOH675
|
3.5
|
23.4
|
1.0
|
NZ
|
A:LYS200
|
3.5
|
16.6
|
1.0
|
CA
|
A:SER110
|
3.7
|
11.9
|
1.0
|
CB
|
A:SER110
|
3.8
|
14.4
|
1.0
|
CA
|
A:ALA174
|
3.8
|
20.7
|
1.0
|
OD1
|
A:ASN168
|
3.8
|
26.2
|
1.0
|
C
|
A:SER110
|
4.0
|
15.5
|
1.0
|
C
|
A:TYR173
|
4.3
|
18.7
|
1.0
|
CA
|
A:GLY111
|
4.3
|
23.0
|
1.0
|
CA
|
A:TYR173
|
4.3
|
24.1
|
1.0
|
CB
|
A:TYR173
|
4.6
|
24.5
|
1.0
|
CZ3
|
A:TRP56
|
4.6
|
18.4
|
1.0
|
CB
|
A:ALA174
|
4.6
|
29.2
|
1.0
|
OG
|
A:SER110
|
4.7
|
23.7
|
1.0
|
CE
|
A:LYS200
|
4.7
|
17.8
|
1.0
|
CG
|
A:ASN168
|
4.9
|
31.0
|
1.0
|
CD1
|
A:TYR173
|
4.9
|
25.4
|
1.0
|
C
|
A:ALA174
|
5.0
|
23.9
|
1.0
|
|
Potassium binding site 2 out
of 4 in 6ys9
Go back to
Potassium Binding Sites List in 6ys9
Potassium binding site 2 out
of 4 in the T_926 Truncate of Chlh From Thermosynechococcus Elongatus at 1.64 A Resolution
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of T_926 Truncate of Chlh From Thermosynechococcus Elongatus at 1.64 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K501
b:25.7
occ:1.00
|
O
|
B:HOH754
|
2.9
|
26.0
|
1.0
|
O
|
B:HOH770
|
3.1
|
25.4
|
1.0
|
N
|
B:ALA174
|
3.2
|
17.0
|
1.0
|
N
|
B:GLY111
|
3.3
|
20.2
|
1.0
|
NZ
|
B:LYS200
|
3.3
|
14.0
|
1.0
|
O
|
B:HOH702
|
3.5
|
23.8
|
1.0
|
CA
|
B:ALA174
|
3.8
|
10.7
|
1.0
|
OD1
|
B:ASN168
|
3.8
|
18.0
|
1.0
|
CA
|
B:SER110
|
3.8
|
20.3
|
1.0
|
CB
|
B:SER110
|
3.9
|
18.5
|
1.0
|
C
|
B:SER110
|
4.1
|
16.4
|
1.0
|
C
|
B:TYR173
|
4.1
|
27.2
|
1.0
|
CA
|
B:TYR173
|
4.2
|
19.9
|
1.0
|
CA
|
B:GLY111
|
4.3
|
12.9
|
1.0
|
O
|
B:HOH608
|
4.4
|
22.8
|
1.0
|
CB
|
B:TYR173
|
4.5
|
13.4
|
1.0
|
CE
|
B:LYS200
|
4.5
|
23.0
|
1.0
|
CZ3
|
B:TRP56
|
4.7
|
14.4
|
1.0
|
CB
|
B:ALA174
|
4.8
|
15.1
|
1.0
|
CG
|
B:ASN168
|
4.8
|
15.5
|
1.0
|
C
|
B:ALA174
|
4.9
|
21.2
|
1.0
|
OG
|
B:SER110
|
4.9
|
17.0
|
1.0
|
CD1
|
B:TYR173
|
4.9
|
22.8
|
1.0
|
|
Potassium binding site 3 out
of 4 in 6ys9
Go back to
Potassium Binding Sites List in 6ys9
Potassium binding site 3 out
of 4 in the T_926 Truncate of Chlh From Thermosynechococcus Elongatus at 1.64 A Resolution
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of T_926 Truncate of Chlh From Thermosynechococcus Elongatus at 1.64 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K501
b:27.7
occ:1.00
|
O
|
C:HOH688
|
2.9
|
26.9
|
1.0
|
N
|
C:GLY111
|
3.1
|
20.0
|
1.0
|
N
|
C:ALA174
|
3.2
|
14.6
|
1.0
|
O
|
C:HOH660
|
3.5
|
23.3
|
1.0
|
NZ
|
C:LYS200
|
3.7
|
12.9
|
1.0
|
OD1
|
C:ASN168
|
3.8
|
16.8
|
1.0
|
CA
|
C:SER110
|
3.8
|
11.9
|
1.0
|
CA
|
C:ALA174
|
3.9
|
21.9
|
1.0
|
CB
|
C:SER110
|
3.9
|
20.0
|
1.0
|
C
|
C:SER110
|
4.0
|
14.2
|
1.0
|
CA
|
C:GLY111
|
4.0
|
25.5
|
1.0
|
C
|
C:TYR173
|
4.1
|
16.9
|
1.0
|
CA
|
C:TYR173
|
4.1
|
10.9
|
1.0
|
O
|
C:HOH605
|
4.4
|
21.5
|
1.0
|
CB
|
C:TYR173
|
4.5
|
20.9
|
1.0
|
CG
|
C:ASN168
|
4.7
|
16.6
|
1.0
|
CE
|
C:LYS200
|
4.7
|
16.3
|
1.0
|
CZ3
|
C:TRP56
|
4.8
|
16.4
|
1.0
|
OG
|
C:SER110
|
4.8
|
18.2
|
1.0
|
CB
|
C:ALA174
|
4.8
|
24.1
|
1.0
|
CD2
|
C:TYR173
|
4.9
|
17.7
|
1.0
|
C
|
C:ALA174
|
4.9
|
16.9
|
1.0
|
|
Potassium binding site 4 out
of 4 in 6ys9
Go back to
Potassium Binding Sites List in 6ys9
Potassium binding site 4 out
of 4 in the T_926 Truncate of Chlh From Thermosynechococcus Elongatus at 1.64 A Resolution
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of T_926 Truncate of Chlh From Thermosynechococcus Elongatus at 1.64 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K501
b:23.3
occ:1.00
|
O
|
D:HOH724
|
3.0
|
16.3
|
1.0
|
N
|
D:ALA174
|
3.1
|
14.0
|
1.0
|
O
|
D:HOH752
|
3.1
|
26.5
|
1.0
|
N
|
D:GLY111
|
3.2
|
12.8
|
1.0
|
O
|
D:HOH659
|
3.3
|
22.1
|
1.0
|
NZ
|
D:LYS200
|
3.4
|
15.1
|
1.0
|
CA
|
D:ALA174
|
3.7
|
25.3
|
1.0
|
OD1
|
D:ASN168
|
3.7
|
15.8
|
1.0
|
CA
|
D:SER110
|
3.7
|
15.3
|
1.0
|
CB
|
D:SER110
|
3.8
|
12.3
|
1.0
|
C
|
D:SER110
|
3.9
|
12.5
|
1.0
|
C
|
D:TYR173
|
4.1
|
15.0
|
1.0
|
CA
|
D:TYR173
|
4.1
|
9.1
|
1.0
|
CA
|
D:GLY111
|
4.1
|
17.3
|
1.0
|
CB
|
D:TYR173
|
4.4
|
14.5
|
1.0
|
CB
|
D:ALA174
|
4.5
|
17.8
|
1.0
|
CG
|
D:ASN168
|
4.6
|
13.8
|
1.0
|
O
|
D:HOH611
|
4.6
|
19.5
|
1.0
|
CE
|
D:LYS200
|
4.7
|
17.3
|
1.0
|
CZ3
|
D:TRP56
|
4.7
|
13.5
|
1.0
|
OG
|
D:SER110
|
4.9
|
14.6
|
1.0
|
CD1
|
D:TYR173
|
4.9
|
14.4
|
1.0
|
C
|
D:ALA174
|
4.9
|
14.5
|
1.0
|
|
Reference:
N.B.P.Adams,
C.Bisson,
A.A.Brindley,
D.A.Farmer,
P.A.Davison,
J.D.Reid,
C.N.Hunter.
The Active Site of Magnesium Chelatase. Nat.Plants 2020.
ISSN: ESSN 2055-0278
PubMed: 33257858
DOI: 10.1038/S41477-020-00806-9
Page generated: Mon Aug 12 18:27:14 2024
|