Thallium in PDB 1f1h: Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions
Enzymatic activity of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions
All present enzymatic activity of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions:
6.3.1.2;
Protein crystallography data
The structure of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions, PDB code: 1f1h
was solved by
H.S.Gill,
D.Eisenberg,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
32.00 /
2.67
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
231.130,
132.790,
196.780,
90.00,
102.44,
90.00
|
R / Rfree (%)
|
23.2 /
26.3
|
Other elements in 1f1h:
The structure of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions also contains other interesting chemical elements:
Thallium Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
20;
Page 3, Binding sites: 21 -
24;
Binding sites:
The binding sites of Thallium atom in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions
(pdb code 1f1h). This binding sites where shown within
5.0 Angstroms radius around Thallium atom.
In total 24 binding sites of Thallium where determined in the
Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions, PDB code: 1f1h:
Jump to Thallium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Thallium binding site 1 out
of 24 in 1f1h
Go back to
Thallium Binding Sites List in 1f1h
Thallium binding site 1 out
of 24 in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions
Mono view
Stereo pair view
|
A full contact list of Thallium with other atoms in the Tl binding
site number 1 of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Tl473
b:67.6
occ:0.39
|
OH
|
A:TYR179
|
2.9
|
86.1
|
0.4
|
OE2
|
A:GLU212
|
3.0
|
36.5
|
1.0
|
OE1
|
A:GLU212
|
3.1
|
40.3
|
1.0
|
OG
|
B:SER53
|
3.1
|
55.6
|
0.4
|
CZ
|
A:TYR179
|
3.2
|
68.5
|
0.4
|
OD1
|
B:ASP50
|
3.2
|
81.2
|
0.4
|
CD
|
A:GLU212
|
3.4
|
39.6
|
1.0
|
O
|
A:HOH1583
|
3.6
|
49.4
|
1.0
|
CE2
|
A:TYR179
|
3.7
|
64.9
|
0.4
|
OD2
|
B:ASP50
|
3.7
|
76.7
|
0.4
|
CB
|
B:SER53
|
3.8
|
64.2
|
0.4
|
MN
|
A:MN469
|
3.8
|
34.9
|
1.0
|
CG
|
B:ASP50
|
3.9
|
79.0
|
0.4
|
CE1
|
A:TYR179
|
3.9
|
78.7
|
0.4
|
CG2
|
A:VAL213
|
4.0
|
28.0
|
1.0
|
O
|
B:HOH1490
|
4.4
|
67.0
|
1.0
|
CD2
|
A:TYR179
|
4.6
|
52.2
|
0.4
|
OE1
|
A:GLU131
|
4.6
|
40.2
|
1.0
|
O
|
B:ASP50
|
4.8
|
41.7
|
0.4
|
CD1
|
A:TYR179
|
4.8
|
60.5
|
0.4
|
CG
|
A:GLU212
|
4.9
|
26.5
|
1.0
|
|
Thallium binding site 2 out
of 24 in 1f1h
Go back to
Thallium Binding Sites List in 1f1h
Thallium binding site 2 out
of 24 in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions
Mono view
Stereo pair view
|
A full contact list of Thallium with other atoms in the Tl binding
site number 2 of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Tl474
b:75.1
occ:0.39
|
OE2
|
A:GLU131
|
2.7
|
32.2
|
1.0
|
O
|
A:HOH1584
|
2.9
|
48.4
|
1.0
|
OD1
|
A:ASN264
|
3.0
|
65.7
|
1.0
|
O
|
A:GLY265
|
3.1
|
36.4
|
1.0
|
O
|
A:HOH1554
|
3.3
|
53.2
|
1.0
|
CD
|
A:GLU131
|
3.4
|
37.3
|
1.0
|
OE1
|
A:GLU131
|
3.4
|
40.2
|
1.0
|
CG
|
A:ASN264
|
4.0
|
53.5
|
1.0
|
C
|
A:GLY265
|
4.2
|
25.4
|
1.0
|
N
|
A:GLY267
|
4.2
|
35.8
|
1.0
|
OE1
|
A:GLU212
|
4.2
|
40.3
|
1.0
|
NE2
|
A:GLN218
|
4.3
|
15.7
|
1.0
|
OE1
|
A:GLN218
|
4.3
|
38.9
|
1.0
|
O
|
A:HOH1573
|
4.5
|
34.4
|
1.0
|
O
|
A:HOH1495
|
4.5
|
24.0
|
1.0
|
CA
|
A:SER266
|
4.5
|
26.0
|
1.0
|
CD
|
A:GLN218
|
4.8
|
15.3
|
1.0
|
CG
|
A:GLU131
|
4.8
|
24.8
|
1.0
|
ND2
|
A:ASN264
|
4.8
|
31.9
|
1.0
|
C
|
A:SER266
|
4.8
|
33.4
|
1.0
|
CB
|
A:ASN264
|
4.8
|
49.0
|
1.0
|
CD
|
A:GLU212
|
4.8
|
39.6
|
1.0
|
N
|
A:SER266
|
4.8
|
25.7
|
1.0
|
N
|
A:GLY265
|
4.9
|
28.7
|
1.0
|
|
Thallium binding site 3 out
of 24 in 1f1h
Go back to
Thallium Binding Sites List in 1f1h
Thallium binding site 3 out
of 24 in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions
Mono view
Stereo pair view
|
A full contact list of Thallium with other atoms in the Tl binding
site number 3 of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Tl473
b:67.6
occ:0.39
|
OH
|
B:TYR179
|
2.9
|
86.1
|
0.4
|
OE2
|
B:GLU212
|
3.0
|
36.5
|
1.0
|
OE1
|
B:GLU212
|
3.1
|
40.3
|
1.0
|
OD1
|
C:ASP50
|
3.2
|
81.2
|
0.4
|
CZ
|
B:TYR179
|
3.2
|
68.5
|
0.4
|
OG
|
C:SER53
|
3.3
|
55.6
|
0.4
|
CD
|
B:GLU212
|
3.4
|
39.6
|
1.0
|
O
|
B:HOH1590
|
3.6
|
49.4
|
1.0
|
CE2
|
B:TYR179
|
3.7
|
64.9
|
0.4
|
OD2
|
C:ASP50
|
3.7
|
76.7
|
0.4
|
MN
|
B:MN469
|
3.8
|
34.9
|
1.0
|
CG
|
C:ASP50
|
3.9
|
79.0
|
0.4
|
CE1
|
B:TYR179
|
3.9
|
78.7
|
0.4
|
CB
|
C:SER53
|
4.0
|
64.2
|
0.4
|
CG2
|
B:VAL213
|
4.0
|
28.0
|
1.0
|
O
|
C:HOH1492
|
4.4
|
67.0
|
1.0
|
CD2
|
B:TYR179
|
4.6
|
52.2
|
0.4
|
OE1
|
B:GLU131
|
4.6
|
40.2
|
1.0
|
CD1
|
B:TYR179
|
4.8
|
60.5
|
0.4
|
O
|
C:ASP50
|
4.9
|
41.7
|
0.4
|
CG
|
B:GLU212
|
4.9
|
26.5
|
1.0
|
|
Thallium binding site 4 out
of 24 in 1f1h
Go back to
Thallium Binding Sites List in 1f1h
Thallium binding site 4 out
of 24 in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions
Mono view
Stereo pair view
|
A full contact list of Thallium with other atoms in the Tl binding
site number 4 of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Tl474
b:75.1
occ:0.39
|
OE2
|
B:GLU131
|
2.7
|
32.2
|
1.0
|
O
|
B:HOH1591
|
2.9
|
48.4
|
1.0
|
OD1
|
B:ASN264
|
3.0
|
65.7
|
1.0
|
O
|
B:GLY265
|
3.1
|
36.4
|
1.0
|
O
|
B:HOH1562
|
3.3
|
53.2
|
1.0
|
CD
|
B:GLU131
|
3.4
|
37.3
|
1.0
|
OE1
|
B:GLU131
|
3.4
|
40.2
|
1.0
|
CG
|
B:ASN264
|
4.0
|
53.5
|
1.0
|
C
|
B:GLY265
|
4.2
|
25.4
|
1.0
|
N
|
B:GLY267
|
4.2
|
35.8
|
1.0
|
OE1
|
B:GLU212
|
4.2
|
40.3
|
1.0
|
NE2
|
B:GLN218
|
4.3
|
15.7
|
1.0
|
OE1
|
B:GLN218
|
4.3
|
38.9
|
1.0
|
O
|
B:HOH1580
|
4.5
|
34.4
|
1.0
|
O
|
B:HOH1502
|
4.5
|
24.0
|
1.0
|
CA
|
B:SER266
|
4.5
|
26.0
|
1.0
|
CD
|
B:GLN218
|
4.8
|
15.3
|
1.0
|
CG
|
B:GLU131
|
4.8
|
24.8
|
1.0
|
ND2
|
B:ASN264
|
4.8
|
31.9
|
1.0
|
C
|
B:SER266
|
4.8
|
33.4
|
1.0
|
CB
|
B:ASN264
|
4.8
|
49.0
|
1.0
|
CD
|
B:GLU212
|
4.8
|
39.6
|
1.0
|
N
|
B:SER266
|
4.8
|
25.7
|
1.0
|
N
|
B:GLY265
|
4.9
|
28.7
|
1.0
|
|
Thallium binding site 5 out
of 24 in 1f1h
Go back to
Thallium Binding Sites List in 1f1h
Thallium binding site 5 out
of 24 in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions
Mono view
Stereo pair view
|
A full contact list of Thallium with other atoms in the Tl binding
site number 5 of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Tl473
b:67.6
occ:0.39
|
OH
|
C:TYR179
|
2.9
|
86.1
|
0.4
|
OE2
|
C:GLU212
|
3.0
|
36.5
|
1.0
|
OG
|
D:SER53
|
3.0
|
55.6
|
0.4
|
OD1
|
D:ASP50
|
3.1
|
81.2
|
0.4
|
OE1
|
C:GLU212
|
3.1
|
40.3
|
1.0
|
CZ
|
C:TYR179
|
3.2
|
68.5
|
0.4
|
CD
|
C:GLU212
|
3.4
|
39.6
|
1.0
|
O
|
D:HOH1494
|
3.6
|
49.4
|
1.0
|
OD2
|
D:ASP50
|
3.6
|
76.7
|
0.4
|
CE2
|
C:TYR179
|
3.7
|
64.9
|
0.4
|
CB
|
D:SER53
|
3.7
|
64.2
|
0.4
|
CG
|
D:ASP50
|
3.8
|
79.0
|
0.4
|
MN
|
C:MN469
|
3.8
|
34.9
|
1.0
|
CE1
|
C:TYR179
|
3.9
|
78.7
|
0.4
|
CG2
|
C:VAL213
|
4.0
|
28.0
|
1.0
|
O
|
D:HOH1493
|
4.4
|
67.0
|
1.0
|
CD2
|
C:TYR179
|
4.6
|
52.2
|
0.4
|
OE1
|
C:GLU131
|
4.6
|
40.2
|
1.0
|
O
|
D:ASP50
|
4.7
|
41.7
|
0.4
|
CD1
|
C:TYR179
|
4.8
|
60.5
|
0.4
|
CG
|
C:GLU212
|
4.9
|
26.5
|
1.0
|
|
Thallium binding site 6 out
of 24 in 1f1h
Go back to
Thallium Binding Sites List in 1f1h
Thallium binding site 6 out
of 24 in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions
Mono view
Stereo pair view
|
A full contact list of Thallium with other atoms in the Tl binding
site number 6 of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Tl474
b:75.1
occ:0.39
|
OE2
|
C:GLU131
|
2.7
|
32.2
|
1.0
|
O
|
C:HOH1591
|
2.9
|
48.4
|
1.0
|
OD1
|
C:ASN264
|
3.0
|
65.7
|
1.0
|
O
|
C:GLY265
|
3.1
|
36.4
|
1.0
|
O
|
C:HOH1563
|
3.3
|
53.2
|
1.0
|
CD
|
C:GLU131
|
3.4
|
37.3
|
1.0
|
OE1
|
C:GLU131
|
3.4
|
40.2
|
1.0
|
CG
|
C:ASN264
|
4.0
|
53.5
|
1.0
|
C
|
C:GLY265
|
4.2
|
25.4
|
1.0
|
N
|
C:GLY267
|
4.2
|
35.8
|
1.0
|
OE1
|
C:GLU212
|
4.2
|
40.3
|
1.0
|
NE2
|
C:GLN218
|
4.3
|
15.7
|
1.0
|
OE1
|
C:GLN218
|
4.3
|
38.9
|
1.0
|
O
|
C:HOH1581
|
4.5
|
34.4
|
1.0
|
O
|
C:HOH1504
|
4.5
|
24.0
|
1.0
|
CA
|
C:SER266
|
4.5
|
26.0
|
1.0
|
CD
|
C:GLN218
|
4.8
|
15.3
|
1.0
|
CG
|
C:GLU131
|
4.8
|
24.8
|
1.0
|
ND2
|
C:ASN264
|
4.8
|
31.9
|
1.0
|
C
|
C:SER266
|
4.8
|
33.4
|
1.0
|
CB
|
C:ASN264
|
4.8
|
49.0
|
1.0
|
CD
|
C:GLU212
|
4.8
|
39.6
|
1.0
|
N
|
C:SER266
|
4.8
|
25.7
|
1.0
|
N
|
C:GLY265
|
4.9
|
28.7
|
1.0
|
|
Thallium binding site 7 out
of 24 in 1f1h
Go back to
Thallium Binding Sites List in 1f1h
Thallium binding site 7 out
of 24 in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions
Mono view
Stereo pair view
|
A full contact list of Thallium with other atoms in the Tl binding
site number 7 of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Tl473
b:67.6
occ:0.39
|
OH
|
D:TYR179
|
2.9
|
86.1
|
0.4
|
OE2
|
D:GLU212
|
3.0
|
36.5
|
1.0
|
OD1
|
E:ASP50
|
3.1
|
81.2
|
0.4
|
OG
|
E:SER53
|
3.1
|
55.6
|
0.4
|
OE1
|
D:GLU212
|
3.1
|
40.3
|
1.0
|
CZ
|
D:TYR179
|
3.2
|
68.5
|
0.4
|
CD
|
D:GLU212
|
3.4
|
39.6
|
1.0
|
O
|
D:HOH1595
|
3.6
|
49.4
|
1.0
|
OD2
|
E:ASP50
|
3.6
|
76.7
|
0.4
|
CE2
|
D:TYR179
|
3.7
|
64.9
|
0.4
|
CG
|
E:ASP50
|
3.7
|
79.0
|
0.4
|
MN
|
D:MN469
|
3.8
|
34.9
|
1.0
|
CB
|
E:SER53
|
3.8
|
64.2
|
0.4
|
CE1
|
D:TYR179
|
3.9
|
78.7
|
0.4
|
CG2
|
D:VAL213
|
4.0
|
28.0
|
1.0
|
O
|
E:HOH1493
|
4.4
|
67.0
|
1.0
|
CD2
|
D:TYR179
|
4.6
|
52.2
|
0.4
|
OE1
|
D:GLU131
|
4.6
|
40.2
|
1.0
|
O
|
E:ASP50
|
4.7
|
41.7
|
0.4
|
CD1
|
D:TYR179
|
4.8
|
60.5
|
0.4
|
CG
|
D:GLU212
|
4.9
|
26.5
|
1.0
|
|
Thallium binding site 8 out
of 24 in 1f1h
Go back to
Thallium Binding Sites List in 1f1h
Thallium binding site 8 out
of 24 in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions
Mono view
Stereo pair view
|
A full contact list of Thallium with other atoms in the Tl binding
site number 8 of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Tl474
b:75.1
occ:0.39
|
OE2
|
D:GLU131
|
2.7
|
32.2
|
1.0
|
O
|
D:HOH1596
|
2.9
|
48.4
|
1.0
|
OD1
|
D:ASN264
|
3.0
|
65.7
|
1.0
|
O
|
D:GLY265
|
3.1
|
36.4
|
1.0
|
O
|
D:HOH1566
|
3.3
|
53.2
|
1.0
|
CD
|
D:GLU131
|
3.4
|
37.3
|
1.0
|
OE1
|
D:GLU131
|
3.4
|
40.2
|
1.0
|
CG
|
D:ASN264
|
4.0
|
53.5
|
1.0
|
C
|
D:GLY265
|
4.2
|
25.4
|
1.0
|
N
|
D:GLY267
|
4.2
|
35.8
|
1.0
|
OE1
|
D:GLU212
|
4.2
|
40.3
|
1.0
|
NE2
|
D:GLN218
|
4.3
|
15.7
|
1.0
|
OE1
|
D:GLN218
|
4.3
|
38.9
|
1.0
|
O
|
D:HOH1585
|
4.5
|
34.4
|
1.0
|
O
|
D:HOH1506
|
4.5
|
24.0
|
1.0
|
CA
|
D:SER266
|
4.5
|
26.0
|
1.0
|
CD
|
D:GLN218
|
4.8
|
15.3
|
1.0
|
CG
|
D:GLU131
|
4.8
|
24.8
|
1.0
|
ND2
|
D:ASN264
|
4.8
|
31.9
|
1.0
|
C
|
D:SER266
|
4.8
|
33.4
|
1.0
|
CB
|
D:ASN264
|
4.8
|
49.0
|
1.0
|
CD
|
D:GLU212
|
4.8
|
39.6
|
1.0
|
N
|
D:SER266
|
4.8
|
25.7
|
1.0
|
N
|
D:GLY265
|
4.9
|
28.7
|
1.0
|
|
Thallium binding site 9 out
of 24 in 1f1h
Go back to
Thallium Binding Sites List in 1f1h
Thallium binding site 9 out
of 24 in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions
Mono view
Stereo pair view
|
A full contact list of Thallium with other atoms in the Tl binding
site number 9 of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Tl473
b:67.6
occ:0.39
|
OH
|
E:TYR179
|
2.9
|
86.1
|
0.4
|
OE2
|
E:GLU212
|
3.0
|
36.5
|
1.0
|
OE1
|
E:GLU212
|
3.1
|
40.3
|
1.0
|
CZ
|
E:TYR179
|
3.2
|
68.5
|
0.4
|
OD1
|
F:ASP50
|
3.3
|
81.2
|
0.4
|
OG
|
F:SER53
|
3.3
|
55.6
|
0.4
|
CD
|
E:GLU212
|
3.4
|
39.6
|
1.0
|
O
|
E:HOH1592
|
3.6
|
49.4
|
1.0
|
CE2
|
E:TYR179
|
3.7
|
64.9
|
0.4
|
OD2
|
F:ASP50
|
3.7
|
76.7
|
0.4
|
MN
|
E:MN469
|
3.8
|
34.9
|
1.0
|
CG
|
F:ASP50
|
3.9
|
79.0
|
0.4
|
CE1
|
E:TYR179
|
3.9
|
78.7
|
0.4
|
CG2
|
E:VAL213
|
4.0
|
28.0
|
1.0
|
CB
|
F:SER53
|
4.0
|
64.2
|
0.4
|
O
|
F:HOH1496
|
4.4
|
67.0
|
1.0
|
CD2
|
E:TYR179
|
4.6
|
52.2
|
0.4
|
OE1
|
E:GLU131
|
4.6
|
40.2
|
1.0
|
CD1
|
E:TYR179
|
4.8
|
60.5
|
0.4
|
CG
|
E:GLU212
|
4.9
|
26.5
|
1.0
|
O
|
F:ASP50
|
5.0
|
41.7
|
0.4
|
|
Thallium binding site 10 out
of 24 in 1f1h
Go back to
Thallium Binding Sites List in 1f1h
Thallium binding site 10 out
of 24 in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions
Mono view
Stereo pair view
|
A full contact list of Thallium with other atoms in the Tl binding
site number 10 of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Tl474
b:75.1
occ:0.39
|
OE2
|
E:GLU131
|
2.7
|
32.2
|
1.0
|
O
|
E:HOH1593
|
2.9
|
48.4
|
1.0
|
OD1
|
E:ASN264
|
3.0
|
65.7
|
1.0
|
O
|
E:GLY265
|
3.1
|
36.4
|
1.0
|
O
|
E:HOH1564
|
3.3
|
53.2
|
1.0
|
CD
|
E:GLU131
|
3.4
|
37.3
|
1.0
|
OE1
|
E:GLU131
|
3.4
|
40.2
|
1.0
|
CG
|
E:ASN264
|
4.0
|
53.5
|
1.0
|
C
|
E:GLY265
|
4.2
|
25.4
|
1.0
|
N
|
E:GLY267
|
4.2
|
35.8
|
1.0
|
OE1
|
E:GLU212
|
4.2
|
40.3
|
1.0
|
NE2
|
E:GLN218
|
4.3
|
15.7
|
1.0
|
OE1
|
E:GLN218
|
4.3
|
38.9
|
1.0
|
O
|
E:HOH1582
|
4.5
|
34.4
|
1.0
|
O
|
E:HOH1505
|
4.5
|
24.0
|
1.0
|
CA
|
E:SER266
|
4.5
|
26.0
|
1.0
|
CD
|
E:GLN218
|
4.8
|
15.3
|
1.0
|
CG
|
E:GLU131
|
4.8
|
24.8
|
1.0
|
ND2
|
E:ASN264
|
4.8
|
31.9
|
1.0
|
C
|
E:SER266
|
4.8
|
33.4
|
1.0
|
CB
|
E:ASN264
|
4.8
|
49.0
|
1.0
|
CD
|
E:GLU212
|
4.8
|
39.6
|
1.0
|
N
|
E:SER266
|
4.8
|
25.7
|
1.0
|
N
|
E:GLY265
|
4.9
|
28.7
|
1.0
|
|
Reference:
H.S.Gill,
D.Eisenberg.
The Crystal Structure of Phosphinothricin in the Active Site of Glutamine Synthetase Illuminates the Mechanism of Enzymatic Inhibition. Biochemistry V. 40 1903 2001.
ISSN: ISSN 0006-2960
PubMed: 11329256
DOI: 10.1021/BI002438H
Page generated: Wed Dec 16 02:28:36 2020
|