Potassium in PDB 7tcs: M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine
Enzymatic activity of M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine
All present enzymatic activity of M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine:
4.1.99.2;
Protein crystallography data
The structure of M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine, PDB code: 7tcs
was solved by
R.S.Phillips,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
45.27 /
1.37
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
63.55,
82.99,
96.58,
93.73,
105.71,
114.24
|
R / Rfree (%)
|
14.1 /
15.5
|
Other elements in 7tcs:
The structure of M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine
(pdb code 7tcs). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the
M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine, PDB code: 7tcs:
Jump to Potassium binding site number:
1;
2;
3;
4;
Potassium binding site 1 out
of 4 in 7tcs
Go back to
Potassium Binding Sites List in 7tcs
Potassium binding site 1 out
of 4 in the M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K501
b:16.4
occ:1.00
|
O
|
D:HOH753
|
2.7
|
18.1
|
1.0
|
OE1
|
D:GLU69
|
2.8
|
16.4
|
1.0
|
O
|
A:GLY52
|
2.9
|
15.7
|
1.0
|
O
|
A:HOH767
|
2.9
|
17.6
|
1.0
|
O
|
A:ASN262
|
2.9
|
15.7
|
1.0
|
HB3
|
D:GLU69
|
3.0
|
20.4
|
1.0
|
HB3
|
A:ASN262
|
3.1
|
17.4
|
1.0
|
O
|
D:GLU69
|
3.2
|
19.4
|
1.0
|
O
|
A:HOH768
|
3.2
|
19.2
|
1.0
|
HA3
|
A:GLY52
|
3.3
|
18.6
|
1.0
|
HA
|
D:GLU69
|
3.4
|
21.2
|
1.0
|
HA
|
D:ALA295
|
3.5
|
18.0
|
1.0
|
C
|
A:GLY52
|
3.7
|
15.6
|
1.0
|
CB
|
D:GLU69
|
3.8
|
17.0
|
1.0
|
HA
|
A:ASN262
|
3.8
|
17.6
|
1.0
|
H
|
D:GLY296
|
3.8
|
19.2
|
1.0
|
C
|
A:ASN262
|
3.9
|
14.6
|
1.0
|
CD
|
D:GLU69
|
3.9
|
17.4
|
1.0
|
C
|
D:GLU69
|
3.9
|
19.8
|
1.0
|
CA
|
D:GLU69
|
3.9
|
17.6
|
1.0
|
CB
|
A:ASN262
|
3.9
|
14.5
|
1.0
|
CA
|
A:GLY52
|
3.9
|
15.5
|
1.0
|
O
|
D:HOH752
|
4.0
|
20.6
|
1.0
|
CA
|
A:ASN262
|
4.1
|
14.7
|
1.0
|
HE3
|
A:LYS256
|
4.1
|
20.4
|
1.0
|
HA2
|
A:GLY52
|
4.2
|
18.6
|
1.0
|
HD22
|
A:ASN262
|
4.2
|
18.6
|
1.0
|
CG
|
D:GLU69
|
4.3
|
17.5
|
1.0
|
CA
|
D:ALA295
|
4.4
|
15.0
|
1.0
|
HB2
|
A:ASN262
|
4.5
|
17.4
|
1.0
|
HB2
|
D:GLU69
|
4.5
|
20.4
|
1.0
|
N
|
D:GLY296
|
4.6
|
16.0
|
1.0
|
HG3
|
D:GLU69
|
4.6
|
21.1
|
1.0
|
HZ1
|
A:LYS256
|
4.6
|
20.5
|
1.0
|
HB1
|
D:ALA295
|
4.6
|
21.5
|
1.0
|
HE2
|
A:LYS256
|
4.6
|
20.4
|
1.0
|
HA
|
A:THR53
|
4.7
|
18.2
|
1.0
|
N
|
A:THR53
|
4.8
|
15.2
|
1.0
|
CE
|
A:LYS256
|
4.8
|
17.0
|
1.0
|
ND2
|
A:ASN262
|
4.8
|
15.5
|
1.0
|
CG
|
A:ASN262
|
4.9
|
15.0
|
1.0
|
HB2
|
D:ALA295
|
4.9
|
21.5
|
1.0
|
O
|
D:ALA70
|
4.9
|
18.1
|
1.0
|
CB
|
D:ALA295
|
4.9
|
17.9
|
1.0
|
HB
|
A:ILE263
|
4.9
|
18.5
|
1.0
|
OE2
|
D:GLU69
|
5.0
|
16.0
|
1.0
|
O
|
D:LEU294
|
5.0
|
17.7
|
1.0
|
O
|
A:SER51
|
5.0
|
18.7
|
1.0
|
|
Potassium binding site 2 out
of 4 in 7tcs
Go back to
Potassium Binding Sites List in 7tcs
Potassium binding site 2 out
of 4 in the M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K504
b:17.3
occ:1.00
|
O
|
A:HOH757
|
2.7
|
17.5
|
1.0
|
OE1
|
A:GLU69
|
2.7
|
17.1
|
1.0
|
O
|
D:HOH697
|
2.8
|
18.5
|
1.0
|
O
|
D:ASN262
|
2.8
|
16.8
|
1.0
|
O
|
D:GLY52
|
2.9
|
16.5
|
1.0
|
HB3
|
A:GLU69
|
3.0
|
20.2
|
1.0
|
HB3
|
D:ASN262
|
3.1
|
17.5
|
1.0
|
O
|
D:HOH729
|
3.1
|
20.0
|
1.0
|
HA3
|
D:GLY52
|
3.3
|
18.4
|
1.0
|
O
|
A:GLU69
|
3.3
|
19.6
|
1.0
|
HA
|
A:ALA295
|
3.4
|
20.8
|
1.0
|
HA
|
A:GLU69
|
3.5
|
20.4
|
1.0
|
C
|
D:GLY52
|
3.6
|
16.1
|
1.0
|
H
|
A:GLY296
|
3.8
|
19.6
|
1.0
|
HA
|
D:ASN262
|
3.8
|
19.6
|
1.0
|
CB
|
A:GLU69
|
3.8
|
16.8
|
1.0
|
C
|
D:ASN262
|
3.8
|
16.2
|
1.0
|
CD
|
A:GLU69
|
3.8
|
15.6
|
1.0
|
CA
|
D:GLY52
|
3.9
|
15.3
|
1.0
|
CB
|
D:ASN262
|
4.0
|
14.5
|
1.0
|
CA
|
A:GLU69
|
4.0
|
17.0
|
1.0
|
HE3
|
D:LYS256
|
4.0
|
18.1
|
1.0
|
C
|
A:GLU69
|
4.1
|
18.2
|
1.0
|
CA
|
D:ASN262
|
4.1
|
16.4
|
1.0
|
HA2
|
D:GLY52
|
4.2
|
18.4
|
1.0
|
HD22
|
D:ASN262
|
4.2
|
20.1
|
1.0
|
O
|
A:HOH781
|
4.3
|
19.0
|
1.0
|
CG
|
A:GLU69
|
4.3
|
16.8
|
1.0
|
CA
|
A:ALA295
|
4.4
|
17.3
|
1.0
|
HG3
|
A:GLU69
|
4.5
|
20.2
|
1.0
|
N
|
A:GLY296
|
4.5
|
16.3
|
1.0
|
HB2
|
D:ASN262
|
4.5
|
17.5
|
1.0
|
HB2
|
A:GLU69
|
4.6
|
20.2
|
1.0
|
HB1
|
A:ALA295
|
4.6
|
20.3
|
1.0
|
HZ1
|
D:LYS256
|
4.7
|
20.7
|
1.0
|
HE2
|
D:LYS256
|
4.7
|
18.1
|
1.0
|
HA
|
D:THR53
|
4.7
|
18.8
|
1.0
|
CE
|
D:LYS256
|
4.8
|
15.1
|
1.0
|
HB2
|
A:ALA295
|
4.8
|
20.3
|
1.0
|
N
|
D:THR53
|
4.8
|
16.2
|
1.0
|
ND2
|
D:ASN262
|
4.8
|
16.7
|
1.0
|
HB
|
D:ILE263
|
4.8
|
18.1
|
1.0
|
CB
|
A:ALA295
|
4.8
|
16.9
|
1.0
|
O
|
A:LEU294
|
4.9
|
16.7
|
1.0
|
CG
|
D:ASN262
|
4.9
|
15.5
|
1.0
|
O
|
D:SER51
|
4.9
|
16.7
|
1.0
|
OE2
|
A:GLU69
|
4.9
|
16.6
|
1.0
|
C
|
A:ALA295
|
5.0
|
16.5
|
1.0
|
|
Potassium binding site 3 out
of 4 in 7tcs
Go back to
Potassium Binding Sites List in 7tcs
Potassium binding site 3 out
of 4 in the M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K501
b:16.5
occ:1.00
|
O
|
C:HOH764
|
2.7
|
18.0
|
1.0
|
OE1
|
C:GLU69
|
2.7
|
16.0
|
1.0
|
O
|
B:GLY52
|
2.8
|
16.8
|
1.0
|
O
|
B:HOH727
|
2.8
|
17.8
|
1.0
|
O
|
B:ASN262
|
2.9
|
15.3
|
1.0
|
HB3
|
C:GLU69
|
3.0
|
21.4
|
1.0
|
HB3
|
B:ASN262
|
3.0
|
16.8
|
1.0
|
O
|
B:HOH780
|
3.2
|
19.5
|
1.0
|
O
|
C:GLU69
|
3.2
|
18.9
|
1.0
|
HA3
|
B:GLY52
|
3.3
|
19.0
|
1.0
|
HA
|
C:GLU69
|
3.5
|
21.8
|
1.0
|
HA
|
C:ALA295
|
3.5
|
19.1
|
1.0
|
C
|
B:GLY52
|
3.7
|
16.2
|
1.0
|
CB
|
C:GLU69
|
3.7
|
17.8
|
1.0
|
HA
|
B:ASN262
|
3.8
|
16.5
|
1.0
|
H
|
C:GLY296
|
3.8
|
19.5
|
1.0
|
CD
|
C:GLU69
|
3.9
|
17.8
|
1.0
|
C
|
B:ASN262
|
3.9
|
15.3
|
1.0
|
CB
|
B:ASN262
|
3.9
|
14.0
|
1.0
|
CA
|
C:GLU69
|
3.9
|
18.1
|
1.0
|
C
|
C:GLU69
|
3.9
|
18.0
|
1.0
|
CA
|
B:GLY52
|
4.0
|
15.8
|
1.0
|
HE3
|
B:LYS256
|
4.1
|
19.7
|
1.0
|
CA
|
B:ASN262
|
4.1
|
13.8
|
1.0
|
O
|
C:HOH805
|
4.1
|
20.8
|
1.0
|
HD22
|
B:ASN262
|
4.2
|
19.6
|
1.0
|
HA2
|
B:GLY52
|
4.3
|
19.0
|
1.0
|
CG
|
C:GLU69
|
4.3
|
17.1
|
1.0
|
CA
|
C:ALA295
|
4.4
|
15.9
|
1.0
|
HB2
|
B:ASN262
|
4.5
|
16.8
|
1.0
|
HG3
|
C:GLU69
|
4.5
|
20.6
|
1.0
|
HB2
|
C:GLU69
|
4.5
|
21.4
|
1.0
|
N
|
C:GLY296
|
4.5
|
16.2
|
1.0
|
HB1
|
C:ALA295
|
4.6
|
20.0
|
1.0
|
HE2
|
B:LYS256
|
4.7
|
19.7
|
1.0
|
HZ1
|
B:LYS256
|
4.7
|
21.7
|
1.0
|
HA
|
B:THR53
|
4.7
|
19.8
|
1.0
|
N
|
B:THR53
|
4.8
|
15.5
|
1.0
|
ND2
|
B:ASN262
|
4.8
|
16.3
|
1.0
|
CE
|
B:LYS256
|
4.8
|
16.4
|
1.0
|
CG
|
B:ASN262
|
4.8
|
15.7
|
1.0
|
HB2
|
C:ALA295
|
4.9
|
20.0
|
1.0
|
HB
|
B:ILE263
|
4.9
|
17.3
|
1.0
|
CB
|
C:ALA295
|
4.9
|
16.6
|
1.0
|
O
|
C:LEU294
|
4.9
|
16.9
|
1.0
|
OE2
|
C:GLU69
|
4.9
|
17.5
|
1.0
|
O
|
C:ALA70
|
5.0
|
20.1
|
1.0
|
O
|
B:SER51
|
5.0
|
17.5
|
1.0
|
|
Potassium binding site 4 out
of 4 in 7tcs
Go back to
Potassium Binding Sites List in 7tcs
Potassium binding site 4 out
of 4 in the M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of M379A Mutant Tyrosine Phenol-Lyase Complexed with L-Methionine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K505
b:16.2
occ:1.00
|
O
|
B:HOH704
|
2.8
|
18.9
|
1.0
|
OE1
|
B:GLU69
|
2.8
|
16.8
|
1.0
|
O
|
C:GLY52
|
2.9
|
15.8
|
1.0
|
O
|
C:ASN262
|
2.9
|
15.6
|
1.0
|
O
|
C:HOH742
|
2.9
|
17.9
|
1.0
|
HB3
|
B:GLU69
|
3.0
|
19.0
|
1.0
|
HB3
|
C:ASN262
|
3.1
|
17.4
|
1.0
|
O
|
B:GLU69
|
3.1
|
18.0
|
1.0
|
O
|
C:HOH829
|
3.2
|
20.6
|
1.0
|
HA3
|
C:GLY52
|
3.4
|
17.4
|
1.0
|
HA
|
B:GLU69
|
3.4
|
17.7
|
1.0
|
HA
|
B:ALA295
|
3.5
|
19.1
|
1.0
|
C
|
C:GLY52
|
3.7
|
15.7
|
1.0
|
CB
|
B:GLU69
|
3.7
|
15.8
|
1.0
|
HA
|
C:ASN262
|
3.8
|
18.2
|
1.0
|
H
|
B:GLY296
|
3.8
|
19.9
|
1.0
|
C
|
B:GLU69
|
3.8
|
19.8
|
1.0
|
C
|
C:ASN262
|
3.9
|
15.5
|
1.0
|
CA
|
B:GLU69
|
3.9
|
14.7
|
1.0
|
CD
|
B:GLU69
|
3.9
|
16.3
|
1.0
|
CB
|
C:ASN262
|
3.9
|
14.5
|
1.0
|
CA
|
C:GLY52
|
4.0
|
14.5
|
1.0
|
O
|
B:HOH739
|
4.0
|
20.9
|
1.0
|
CA
|
C:ASN262
|
4.1
|
15.2
|
1.0
|
HE3
|
C:LYS256
|
4.1
|
20.4
|
1.0
|
HD22
|
C:ASN262
|
4.2
|
19.8
|
1.0
|
HA2
|
C:GLY52
|
4.3
|
17.4
|
1.0
|
CG
|
B:GLU69
|
4.3
|
18.1
|
1.0
|
CA
|
B:ALA295
|
4.4
|
15.9
|
1.0
|
HB2
|
C:ASN262
|
4.5
|
17.4
|
1.0
|
HB2
|
B:GLU69
|
4.5
|
19.0
|
1.0
|
N
|
B:GLY296
|
4.5
|
16.6
|
1.0
|
HG3
|
B:GLU69
|
4.6
|
21.7
|
1.0
|
HB1
|
B:ALA295
|
4.6
|
19.9
|
1.0
|
HA
|
C:THR53
|
4.7
|
17.9
|
1.0
|
HZ1
|
C:LYS256
|
4.7
|
21.2
|
1.0
|
N
|
C:THR53
|
4.8
|
16.1
|
1.0
|
HE2
|
C:LYS256
|
4.8
|
20.4
|
1.0
|
O
|
B:ALA70
|
4.8
|
17.9
|
1.0
|
HB2
|
B:ALA295
|
4.8
|
19.9
|
1.0
|
ND2
|
C:ASN262
|
4.8
|
16.5
|
1.0
|
CE
|
C:LYS256
|
4.8
|
17.0
|
1.0
|
CG
|
C:ASN262
|
4.9
|
16.3
|
1.0
|
HB
|
C:ILE263
|
4.9
|
18.3
|
1.0
|
CB
|
B:ALA295
|
4.9
|
16.6
|
1.0
|
OE2
|
B:GLU69
|
4.9
|
16.6
|
1.0
|
HA
|
B:TYR71
|
5.0
|
20.8
|
1.0
|
O
|
B:LEU294
|
5.0
|
18.6
|
1.0
|
|
Reference:
R.S.Phillips,
B.Jones,
S.Nash.
M379A Mutant Tyrosine Phenol-Lyase From Citrobacter Freundii Has Altered Conformational Dynamics. Chembiochem V. 23 00028 2022.
ISSN: ESSN 1439-7633
PubMed: 35577764
DOI: 10.1002/CBIC.202200028
Page generated: Mon Aug 12 21:14:50 2024
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