Potassium in PDB 8tkb: Trna 2-Phosphotransferase (TPT1) From Pyrococcus Horikoshii in Complex with 5'-Amp
Protein crystallography data
The structure of Trna 2-Phosphotransferase (TPT1) From Pyrococcus Horikoshii in Complex with 5'-Amp, PDB code: 8tkb
was solved by
A.Jacewicz,
S.Dantuluri,
S.Shuman,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
41.14 /
1.71
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
38.937,
43.665,
122.861,
90,
90,
90
|
R / Rfree (%)
|
18.5 /
20.9
|
Other elements in 8tkb:
The structure of Trna 2-Phosphotransferase (TPT1) From Pyrococcus Horikoshii in Complex with 5'-Amp also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Trna 2-Phosphotransferase (TPT1) From Pyrococcus Horikoshii in Complex with 5'-Amp
(pdb code 8tkb). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the
Trna 2-Phosphotransferase (TPT1) From Pyrococcus Horikoshii in Complex with 5'-Amp, PDB code: 8tkb:
Jump to Potassium binding site number:
1;
2;
3;
4;
Potassium binding site 1 out
of 4 in 8tkb
Go back to
Potassium Binding Sites List in 8tkb
Potassium binding site 1 out
of 4 in the Trna 2-Phosphotransferase (TPT1) From Pyrococcus Horikoshii in Complex with 5'-Amp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Trna 2-Phosphotransferase (TPT1) From Pyrococcus Horikoshii in Complex with 5'-Amp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K203
b:23.7
occ:0.41
|
O
|
A:GLY28
|
2.8
|
25.2
|
1.0
|
O
|
A:LEU13
|
2.8
|
24.9
|
1.0
|
N
|
A:ALA72
|
3.0
|
24.0
|
1.0
|
NE2
|
A:HIS76
|
3.1
|
25.6
|
1.0
|
CD2
|
A:HIS76
|
3.4
|
27.0
|
1.0
|
OH
|
A:TYR78
|
3.5
|
26.0
|
1.0
|
CB
|
A:ARG71
|
3.6
|
24.8
|
1.0
|
C
|
A:LEU13
|
3.6
|
23.1
|
1.0
|
CB
|
A:LEU13
|
3.6
|
22.5
|
1.0
|
CA
|
A:ARG71
|
3.6
|
21.7
|
1.0
|
C
|
A:GLY28
|
3.7
|
24.6
|
1.0
|
O
|
A:ALA72
|
3.7
|
24.1
|
1.0
|
CB
|
A:ALA72
|
3.8
|
23.4
|
1.0
|
C
|
A:ARG71
|
3.8
|
27.5
|
1.0
|
CA
|
A:ALA72
|
3.9
|
22.9
|
1.0
|
CA
|
A:GLY28
|
3.9
|
24.6
|
1.0
|
CA
|
A:LEU13
|
4.0
|
21.5
|
1.0
|
C
|
A:ALA72
|
4.3
|
26.1
|
1.0
|
CE1
|
A:HIS76
|
4.3
|
23.4
|
1.0
|
CD2
|
A:LEU13
|
4.3
|
21.3
|
1.0
|
CG
|
A:LEU13
|
4.5
|
23.7
|
1.0
|
N
|
A:ARG14
|
4.6
|
23.7
|
1.0
|
CZ
|
A:TYR78
|
4.7
|
26.5
|
1.0
|
CG
|
A:HIS76
|
4.7
|
25.7
|
1.0
|
CG
|
A:ARG71
|
4.7
|
25.4
|
1.0
|
N
|
A:PHE29
|
4.9
|
24.8
|
1.0
|
|
Potassium binding site 2 out
of 4 in 8tkb
Go back to
Potassium Binding Sites List in 8tkb
Potassium binding site 2 out
of 4 in the Trna 2-Phosphotransferase (TPT1) From Pyrococcus Horikoshii in Complex with 5'-Amp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Trna 2-Phosphotransferase (TPT1) From Pyrococcus Horikoshii in Complex with 5'-Amp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K204
b:32.8
occ:0.49
|
O1P
|
A:AMP201
|
2.6
|
34.5
|
1.0
|
O
|
A:HOH323
|
2.7
|
31.0
|
1.0
|
N
|
A:HIS119
|
2.9
|
24.4
|
1.0
|
CE1
|
A:HIS95
|
3.4
|
31.6
|
1.0
|
O
|
A:HOH312
|
3.5
|
32.6
|
1.0
|
O
|
A:HOH374
|
3.6
|
43.1
|
1.0
|
CA
|
A:VAL118
|
3.7
|
24.8
|
1.0
|
C
|
A:VAL118
|
3.8
|
30.6
|
1.0
|
ND1
|
A:HIS119
|
3.8
|
33.5
|
1.0
|
P
|
A:AMP201
|
3.8
|
30.2
|
1.0
|
CA
|
A:HIS119
|
3.9
|
25.5
|
1.0
|
CG1
|
A:VAL118
|
3.9
|
30.1
|
1.0
|
CB
|
A:HIS119
|
3.9
|
26.7
|
1.0
|
C5'
|
A:AMP201
|
3.9
|
25.7
|
1.0
|
O
|
A:HIS119
|
3.9
|
27.4
|
1.0
|
O5'
|
A:AMP201
|
3.9
|
29.0
|
1.0
|
ND1
|
A:HIS95
|
4.1
|
25.4
|
1.0
|
CG
|
A:HIS119
|
4.3
|
26.3
|
1.0
|
CB
|
A:VAL118
|
4.3
|
29.6
|
1.0
|
C
|
A:HIS119
|
4.4
|
28.2
|
1.0
|
C3'
|
A:AMP201
|
4.4
|
32.0
|
1.0
|
NE2
|
A:HIS95
|
4.4
|
28.5
|
1.0
|
O
|
A:TYR117
|
4.4
|
32.7
|
1.0
|
C2'
|
A:AMP201
|
4.4
|
33.2
|
1.0
|
O2P
|
A:AMP201
|
4.6
|
32.9
|
1.0
|
C4'
|
A:AMP201
|
4.7
|
32.0
|
1.0
|
CG2
|
A:VAL118
|
4.8
|
33.8
|
1.0
|
N
|
A:VAL118
|
4.8
|
27.8
|
1.0
|
CG2
|
A:ILE110
|
4.9
|
27.1
|
1.0
|
CE1
|
A:HIS119
|
5.0
|
36.0
|
1.0
|
O
|
A:VAL118
|
5.0
|
29.7
|
1.0
|
|
Potassium binding site 3 out
of 4 in 8tkb
Go back to
Potassium Binding Sites List in 8tkb
Potassium binding site 3 out
of 4 in the Trna 2-Phosphotransferase (TPT1) From Pyrococcus Horikoshii in Complex with 5'-Amp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Trna 2-Phosphotransferase (TPT1) From Pyrococcus Horikoshii in Complex with 5'-Amp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K205
b:32.1
occ:0.52
|
O
|
A:VAL55
|
2.9
|
24.7
|
1.0
|
N
|
A:TYR63
|
2.9
|
25.1
|
1.0
|
O
|
A:TYR63
|
2.9
|
25.0
|
1.0
|
C
|
A:GLY61
|
3.4
|
28.2
|
1.0
|
N
|
A:ARG62
|
3.4
|
22.1
|
1.0
|
CA
|
A:TYR63
|
3.5
|
24.2
|
1.0
|
C
|
A:TYR63
|
3.5
|
26.1
|
1.0
|
CA
|
A:GLY61
|
3.5
|
25.4
|
1.0
|
CB
|
A:TYR63
|
3.6
|
20.1
|
1.0
|
CB
|
A:ASP58
|
3.6
|
23.9
|
1.0
|
O
|
A:HOH319
|
3.6
|
35.4
|
1.0
|
C
|
A:VAL55
|
3.7
|
23.0
|
1.0
|
CG1
|
A:VAL55
|
3.8
|
26.4
|
1.0
|
CA
|
A:VAL55
|
3.9
|
22.1
|
1.0
|
C
|
A:ARG62
|
4.0
|
28.8
|
1.0
|
O
|
A:GLY61
|
4.0
|
26.2
|
1.0
|
CD2
|
A:TYR63
|
4.0
|
22.4
|
1.0
|
CG
|
A:TYR63
|
4.2
|
20.4
|
1.0
|
CA
|
A:ARG62
|
4.2
|
26.6
|
1.0
|
CG
|
A:ASP58
|
4.2
|
30.6
|
1.0
|
OD1
|
A:ASP58
|
4.3
|
27.1
|
1.0
|
N
|
A:GLY61
|
4.3
|
29.7
|
1.0
|
CB
|
A:VAL55
|
4.5
|
23.0
|
1.0
|
CA
|
A:ASP58
|
4.7
|
27.9
|
1.0
|
O
|
A:ASP58
|
4.7
|
35.1
|
1.0
|
N
|
A:ASP58
|
4.8
|
28.9
|
1.0
|
CB
|
A:ARG62
|
4.8
|
24.0
|
1.0
|
N
|
A:GLU64
|
4.8
|
24.8
|
1.0
|
NH2
|
A:ARG73
|
4.8
|
23.3
|
0.5
|
O
|
A:ILE54
|
4.9
|
24.4
|
1.0
|
NE
|
A:ARG73
|
4.9
|
29.3
|
0.5
|
|
Potassium binding site 4 out
of 4 in 8tkb
Go back to
Potassium Binding Sites List in 8tkb
Potassium binding site 4 out
of 4 in the Trna 2-Phosphotransferase (TPT1) From Pyrococcus Horikoshii in Complex with 5'-Amp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of Trna 2-Phosphotransferase (TPT1) From Pyrococcus Horikoshii in Complex with 5'-Amp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K206
b:59.4
occ:0.89
|
O
|
A:HOH340
|
2.8
|
37.8
|
1.0
|
CB
|
A:MET106
|
3.9
|
35.9
|
1.0
|
CG
|
A:MET106
|
4.3
|
46.9
|
1.0
|
CA
|
A:LYS103
|
4.6
|
30.1
|
1.0
|
O
|
A:LYS103
|
4.8
|
36.8
|
1.0
|
CG
|
A:LYS103
|
4.8
|
35.9
|
1.0
|
O
|
A:HOH315
|
5.0
|
46.2
|
1.0
|
|
Reference:
A.Jacewicz,
S.Dantuluri,
S.Shuman.
Trna 2-Phosphotransferase (TPT1) From Pyrococcus Horikoshii in Complex with 5'-Amp To Be Published.
Page generated: Tue Aug 13 01:00:07 2024
|