Potassium in PDB 7tdl: M379A Mutant Tyrosine Phenol-Lyase Complexed with 3-Bromo-Dl- Phenylalanine
Enzymatic activity of M379A Mutant Tyrosine Phenol-Lyase Complexed with 3-Bromo-Dl- Phenylalanine
All present enzymatic activity of M379A Mutant Tyrosine Phenol-Lyase Complexed with 3-Bromo-Dl- Phenylalanine:
4.1.99.2;
Protein crystallography data
The structure of M379A Mutant Tyrosine Phenol-Lyase Complexed with 3-Bromo-Dl- Phenylalanine, PDB code: 7tdl
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)
|
58.41 /
1.60
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
61.25,
82.87,
94.33,
113.16,
96.54,
102.21
|
R / Rfree (%)
|
17.7 /
22.1
|
Other elements in 7tdl:
The structure of M379A Mutant Tyrosine Phenol-Lyase Complexed with 3-Bromo-Dl- Phenylalanine also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the M379A Mutant Tyrosine Phenol-Lyase Complexed with 3-Bromo-Dl- Phenylalanine
(pdb code 7tdl). 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 3-Bromo-Dl- Phenylalanine, PDB code: 7tdl:
Jump to Potassium binding site number:
1;
2;
3;
4;
Potassium binding site 1 out
of 4 in 7tdl
Go back to
Potassium Binding Sites List in 7tdl
Potassium binding site 1 out
of 4 in the M379A Mutant Tyrosine Phenol-Lyase Complexed with 3-Bromo-Dl- Phenylalanine
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 3-Bromo-Dl- Phenylalanine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K502
b:22.9
occ:1.00
|
O
|
A:GLY52
|
2.7
|
20.0
|
1.0
|
OE1
|
B:GLU69
|
2.7
|
21.4
|
1.0
|
O
|
B:HOH655
|
2.7
|
23.4
|
1.0
|
O
|
A:HOH713
|
2.8
|
23.4
|
1.0
|
O
|
A:ASN262
|
2.8
|
22.2
|
1.0
|
O
|
A:HOH718
|
3.0
|
21.3
|
1.0
|
HB3
|
A:ASN262
|
3.0
|
23.9
|
1.0
|
HB3
|
B:GLU69
|
3.1
|
27.3
|
1.0
|
O
|
B:GLU69
|
3.3
|
22.7
|
1.0
|
HA3
|
A:GLY52
|
3.3
|
25.2
|
1.0
|
HA
|
B:ALA295
|
3.4
|
27.8
|
1.0
|
HA
|
B:GLU69
|
3.5
|
26.8
|
1.0
|
C
|
A:GLY52
|
3.6
|
21.9
|
1.0
|
HA
|
A:ASN262
|
3.7
|
23.4
|
1.0
|
H
|
B:GLY296
|
3.8
|
24.4
|
1.0
|
CB
|
B:GLU69
|
3.8
|
22.7
|
1.0
|
C
|
A:ASN262
|
3.8
|
20.5
|
1.0
|
CD
|
B:GLU69
|
3.8
|
22.4
|
1.0
|
CB
|
A:ASN262
|
3.9
|
19.9
|
1.0
|
CA
|
A:GLY52
|
3.9
|
21.0
|
1.0
|
HE3
|
A:LYS256
|
4.0
|
25.7
|
1.0
|
CA
|
B:GLU69
|
4.0
|
22.3
|
1.0
|
C
|
B:GLU69
|
4.0
|
23.5
|
1.0
|
CA
|
A:ASN262
|
4.1
|
19.5
|
1.0
|
O
|
B:HOH763
|
4.1
|
23.8
|
1.0
|
HD22
|
A:ASN262
|
4.1
|
25.6
|
1.0
|
HA2
|
A:GLY52
|
4.2
|
25.2
|
1.0
|
CG
|
B:GLU69
|
4.3
|
21.2
|
1.0
|
CA
|
B:ALA295
|
4.3
|
23.2
|
1.0
|
HB2
|
A:ASN262
|
4.4
|
23.9
|
1.0
|
HG3
|
B:GLU69
|
4.4
|
25.4
|
1.0
|
N
|
B:GLY296
|
4.5
|
20.3
|
1.0
|
HB1
|
B:ALA295
|
4.6
|
25.8
|
1.0
|
HB2
|
B:GLU69
|
4.6
|
27.3
|
1.0
|
HZ3
|
A:LYS256
|
4.6
|
26.9
|
1.0
|
HA
|
A:THR53
|
4.7
|
26.1
|
1.0
|
HE2
|
A:LYS256
|
4.7
|
25.7
|
1.0
|
CE
|
A:LYS256
|
4.7
|
21.4
|
1.0
|
ND2
|
A:ASN262
|
4.7
|
21.3
|
1.0
|
N
|
A:THR53
|
4.7
|
20.5
|
1.0
|
HB2
|
B:ALA295
|
4.7
|
25.8
|
1.0
|
HB
|
A:ILE263
|
4.8
|
27.1
|
1.0
|
CG
|
A:ASN262
|
4.8
|
21.1
|
1.0
|
CB
|
B:ALA295
|
4.8
|
21.4
|
1.0
|
HG23
|
A:THR53
|
4.8
|
28.9
|
1.0
|
O
|
B:LEU294
|
4.9
|
23.7
|
1.0
|
O
|
A:SER51
|
4.9
|
20.9
|
1.0
|
OE2
|
B:GLU69
|
4.9
|
19.1
|
1.0
|
HD13
|
A:ILE263
|
5.0
|
28.4
|
1.0
|
C
|
B:ALA295
|
5.0
|
21.7
|
1.0
|
|
Potassium binding site 2 out
of 4 in 7tdl
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Potassium Binding Sites List in 7tdl
Potassium binding site 2 out
of 4 in the M379A Mutant Tyrosine Phenol-Lyase Complexed with 3-Bromo-Dl- Phenylalanine
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 3-Bromo-Dl- Phenylalanine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K503
b:22.4
occ:1.00
|
OE1
|
A:GLU69
|
2.7
|
21.8
|
1.0
|
O
|
A:HOH628
|
2.8
|
21.5
|
1.0
|
O
|
A:HOH678
|
2.8
|
21.7
|
1.0
|
O
|
B:GLY52
|
2.9
|
21.3
|
1.0
|
O
|
B:ASN262
|
2.9
|
22.3
|
1.0
|
HB3
|
B:ASN262
|
2.9
|
23.4
|
1.0
|
O
|
B:HOH701
|
3.0
|
25.1
|
1.0
|
HB3
|
A:GLU69
|
3.0
|
28.5
|
1.0
|
HA
|
A:ALA295
|
3.3
|
26.0
|
1.0
|
O
|
A:GLU69
|
3.3
|
24.8
|
1.0
|
HA3
|
B:GLY52
|
3.4
|
25.1
|
1.0
|
HA
|
A:GLU69
|
3.5
|
27.9
|
1.0
|
C
|
B:GLY52
|
3.6
|
24.7
|
1.0
|
H
|
A:GLY296
|
3.7
|
28.1
|
1.0
|
CB
|
A:GLU69
|
3.8
|
23.8
|
1.0
|
CB
|
B:ASN262
|
3.8
|
19.5
|
1.0
|
C
|
B:ASN262
|
3.8
|
22.4
|
1.0
|
CD
|
A:GLU69
|
3.8
|
23.4
|
1.0
|
HA
|
B:ASN262
|
3.9
|
24.5
|
1.0
|
CA
|
B:GLY52
|
3.9
|
20.9
|
1.0
|
CA
|
A:GLU69
|
4.0
|
23.2
|
1.0
|
C
|
A:GLU69
|
4.1
|
24.2
|
1.0
|
HE3
|
B:LYS256
|
4.1
|
29.2
|
1.0
|
CA
|
B:ASN262
|
4.1
|
20.4
|
1.0
|
HD22
|
B:ASN262
|
4.2
|
25.6
|
1.0
|
CA
|
A:ALA295
|
4.2
|
21.6
|
1.0
|
HA2
|
B:GLY52
|
4.2
|
25.1
|
1.0
|
O
|
A:HOH701
|
4.2
|
21.9
|
1.0
|
CG
|
A:GLU69
|
4.3
|
22.6
|
1.0
|
HB2
|
B:ASN262
|
4.3
|
23.4
|
1.0
|
HG3
|
A:GLU69
|
4.4
|
27.1
|
1.0
|
N
|
A:GLY296
|
4.5
|
23.4
|
1.0
|
HB1
|
A:ALA295
|
4.5
|
25.7
|
1.0
|
HZ3
|
B:LYS256
|
4.5
|
30.3
|
1.0
|
HB2
|
A:GLU69
|
4.6
|
28.5
|
1.0
|
HE2
|
B:LYS256
|
4.6
|
29.2
|
1.0
|
HB2
|
A:ALA295
|
4.6
|
25.7
|
1.0
|
CB
|
A:ALA295
|
4.7
|
21.4
|
1.0
|
HA
|
B:THR53
|
4.7
|
30.2
|
1.0
|
N
|
B:THR53
|
4.7
|
24.1
|
1.0
|
CE
|
B:LYS256
|
4.7
|
24.4
|
1.0
|
ND2
|
B:ASN262
|
4.8
|
21.4
|
1.0
|
CG
|
B:ASN262
|
4.8
|
21.6
|
1.0
|
HB
|
B:ILE263
|
4.8
|
29.5
|
1.0
|
O
|
A:LEU294
|
4.8
|
22.8
|
1.0
|
C
|
A:ALA295
|
4.9
|
21.4
|
1.0
|
O
|
B:SER51
|
4.9
|
24.1
|
1.0
|
OE2
|
A:GLU69
|
4.9
|
20.2
|
1.0
|
|
Potassium binding site 3 out
of 4 in 7tdl
Go back to
Potassium Binding Sites List in 7tdl
Potassium binding site 3 out
of 4 in the M379A Mutant Tyrosine Phenol-Lyase Complexed with 3-Bromo-Dl- Phenylalanine
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 3-Bromo-Dl- Phenylalanine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K505
b:20.6
occ:1.00
|
O
|
D:HOH682
|
2.7
|
19.6
|
1.0
|
O
|
C:GLY52
|
2.8
|
19.6
|
1.0
|
O
|
D:HOH643
|
2.8
|
21.8
|
1.0
|
OE1
|
D:GLU69
|
2.8
|
23.1
|
1.0
|
O
|
C:ASN262
|
2.9
|
18.7
|
1.0
|
HB3
|
C:ASN262
|
2.9
|
23.6
|
1.0
|
HB3
|
D:GLU69
|
3.0
|
27.1
|
1.0
|
O
|
C:HOH743
|
3.1
|
21.4
|
1.0
|
O
|
D:GLU69
|
3.3
|
22.1
|
1.0
|
HA3
|
C:GLY52
|
3.4
|
25.2
|
1.0
|
HA
|
D:ALA295
|
3.4
|
24.2
|
1.0
|
HA
|
D:GLU69
|
3.6
|
28.7
|
1.0
|
C
|
C:GLY52
|
3.6
|
22.8
|
1.0
|
HA
|
C:ASN262
|
3.7
|
23.7
|
1.0
|
H
|
D:GLY296
|
3.8
|
25.5
|
1.0
|
CB
|
C:ASN262
|
3.8
|
19.7
|
1.0
|
CB
|
D:GLU69
|
3.8
|
22.6
|
1.0
|
C
|
C:ASN262
|
3.8
|
20.7
|
1.0
|
CD
|
D:GLU69
|
3.9
|
24.0
|
1.0
|
O
|
D:HOH710
|
4.0
|
23.0
|
1.0
|
CA
|
C:GLY52
|
4.0
|
21.0
|
1.0
|
CA
|
D:GLU69
|
4.0
|
23.9
|
1.0
|
C
|
D:GLU69
|
4.0
|
23.1
|
1.0
|
CA
|
C:ASN262
|
4.0
|
19.8
|
1.0
|
HE3
|
C:LYS256
|
4.2
|
24.0
|
1.0
|
HD22
|
C:ASN262
|
4.2
|
22.3
|
1.0
|
HA2
|
C:GLY52
|
4.3
|
25.2
|
1.0
|
CG
|
D:GLU69
|
4.3
|
24.8
|
1.0
|
HB2
|
C:ASN262
|
4.3
|
23.6
|
1.0
|
CA
|
D:ALA295
|
4.4
|
20.1
|
1.0
|
HE2
|
C:LYS256
|
4.5
|
24.0
|
1.0
|
HG3
|
D:GLU69
|
4.5
|
29.8
|
1.0
|
HZ3
|
C:LYS256
|
4.6
|
24.7
|
1.0
|
N
|
D:GLY296
|
4.6
|
21.2
|
1.0
|
HB2
|
D:GLU69
|
4.6
|
27.1
|
1.0
|
HA
|
C:THR53
|
4.6
|
28.7
|
1.0
|
HB2
|
D:ALA295
|
4.6
|
24.3
|
1.0
|
HB1
|
D:ALA295
|
4.7
|
24.3
|
1.0
|
N
|
C:THR53
|
4.7
|
21.6
|
1.0
|
CE
|
C:LYS256
|
4.7
|
20.0
|
1.0
|
ND2
|
C:ASN262
|
4.7
|
18.6
|
1.0
|
CG
|
C:ASN262
|
4.8
|
19.4
|
1.0
|
CB
|
D:ALA295
|
4.8
|
20.3
|
1.0
|
O
|
C:SER51
|
4.8
|
23.2
|
1.0
|
O
|
D:ALA70
|
4.9
|
21.0
|
1.0
|
O
|
D:LEU294
|
4.9
|
21.4
|
1.0
|
HB
|
C:ILE263
|
5.0
|
28.6
|
1.0
|
OE2
|
D:GLU69
|
5.0
|
21.2
|
1.0
|
HG23
|
C:THR53
|
5.0
|
28.4
|
1.0
|
|
Potassium binding site 4 out
of 4 in 7tdl
Go back to
Potassium Binding Sites List in 7tdl
Potassium binding site 4 out
of 4 in the M379A Mutant Tyrosine Phenol-Lyase Complexed with 3-Bromo-Dl- Phenylalanine
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 3-Bromo-Dl- Phenylalanine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K506
b:21.2
occ:1.00
|
O
|
C:HOH693
|
2.7
|
22.0
|
1.0
|
O
|
C:HOH784
|
2.7
|
21.9
|
1.0
|
OE1
|
C:GLU69
|
2.7
|
20.4
|
1.0
|
O
|
D:ASN262
|
2.9
|
21.0
|
1.0
|
O
|
D:GLY52
|
2.9
|
21.7
|
1.0
|
HB3
|
C:GLU69
|
2.9
|
24.8
|
1.0
|
HB3
|
D:ASN262
|
3.0
|
24.7
|
1.0
|
O
|
D:HOH716
|
3.2
|
21.8
|
1.0
|
O
|
C:GLU69
|
3.3
|
21.3
|
1.0
|
HA3
|
D:GLY52
|
3.4
|
28.8
|
1.0
|
HA
|
C:ALA295
|
3.5
|
29.5
|
1.0
|
HA
|
C:GLU69
|
3.5
|
28.1
|
1.0
|
C
|
D:GLY52
|
3.7
|
23.8
|
1.0
|
CB
|
C:GLU69
|
3.7
|
20.6
|
1.0
|
H
|
C:GLY296
|
3.8
|
25.3
|
1.0
|
HA
|
D:ASN262
|
3.8
|
25.6
|
1.0
|
CD
|
C:GLU69
|
3.9
|
21.2
|
1.0
|
C
|
D:ASN262
|
3.9
|
19.7
|
1.0
|
CB
|
D:ASN262
|
3.9
|
20.6
|
1.0
|
CA
|
C:GLU69
|
3.9
|
23.4
|
1.0
|
C
|
C:GLU69
|
3.9
|
23.6
|
1.0
|
CA
|
D:GLY52
|
4.0
|
24.0
|
1.0
|
HD22
|
D:ASN262
|
4.1
|
23.9
|
1.0
|
CA
|
D:ASN262
|
4.1
|
21.3
|
1.0
|
HE3
|
D:LYS256
|
4.1
|
25.4
|
1.0
|
O
|
C:HOH766
|
4.1
|
24.1
|
1.0
|
CG
|
C:GLU69
|
4.3
|
20.6
|
1.0
|
HA2
|
D:GLY52
|
4.3
|
28.8
|
1.0
|
CA
|
C:ALA295
|
4.4
|
24.6
|
1.0
|
HB2
|
D:ASN262
|
4.5
|
24.7
|
1.0
|
HB2
|
C:GLU69
|
4.5
|
24.8
|
1.0
|
N
|
C:GLY296
|
4.5
|
21.1
|
1.0
|
HB1
|
C:ALA295
|
4.6
|
25.1
|
1.0
|
HZ3
|
D:LYS256
|
4.6
|
25.6
|
1.0
|
HG3
|
C:GLU69
|
4.6
|
24.8
|
1.0
|
HA
|
D:THR53
|
4.7
|
25.1
|
1.0
|
ND2
|
D:ASN262
|
4.7
|
19.9
|
1.0
|
N
|
D:THR53
|
4.7
|
21.7
|
1.0
|
HE2
|
D:LYS256
|
4.8
|
25.4
|
1.0
|
CG
|
D:ASN262
|
4.8
|
20.6
|
1.0
|
O
|
D:SER51
|
4.8
|
21.0
|
1.0
|
CE
|
D:LYS256
|
4.8
|
21.2
|
1.0
|
HB
|
D:ILE263
|
4.8
|
26.6
|
1.0
|
HG23
|
D:THR53
|
4.9
|
30.9
|
1.0
|
CB
|
C:ALA295
|
4.9
|
20.9
|
1.0
|
HB2
|
C:ALA295
|
4.9
|
25.1
|
1.0
|
O
|
C:ALA70
|
4.9
|
22.4
|
1.0
|
O
|
C:LEU294
|
4.9
|
23.2
|
1.0
|
OE2
|
C:GLU69
|
4.9
|
21.4
|
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 21:15:21 2024
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