Arsenic in PDB 2v98: Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place
Enzymatic activity of Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place
All present enzymatic activity of Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place:
3.1.1.7;
Protein crystallography data
The structure of Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place, PDB code: 2v98
was solved by
J.-P.Colletier,
B.Sanson,
A.Royant,
A.Specht,
F.Nachon,
P.Masson,
G.Zaccai,
J.L.Sussman,
M.Goeldner,
I.Silman,
D.Bourgeois,
M.Weik,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
8.00 /
3.00
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
91.620,
104.470,
148.800,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
20.2 /
24.9
|
Other elements in 2v98:
The structure of Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place also contains other interesting chemical elements:
Arsenic Binding Sites:
The binding sites of Arsenic atom in the Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place
(pdb code 2v98). This binding sites where shown within
5.0 Angstroms radius around Arsenic atom.
In total 8 binding sites of Arsenic where determined in the
Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place, PDB code: 2v98:
Jump to Arsenic binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Arsenic binding site 1 out
of 8 in 2v98
Go back to
Arsenic Binding Sites List in 2v98
Arsenic binding site 1 out
of 8 in the Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place
Mono view
Stereo pair view
|
A full contact list of Arsenic with other atoms in the As binding
site number 1 of Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:As1537
b:52.6
occ:0.80
|
AS
|
A:CFQ1537
|
0.0
|
52.6
|
0.8
|
C4
|
A:CFQ1537
|
1.4
|
47.1
|
0.2
|
AS
|
A:CFQ1537
|
1.7
|
50.1
|
0.2
|
C5
|
A:CFQ1537
|
1.7
|
45.3
|
0.2
|
O1
|
A:CFQ1537
|
2.1
|
43.4
|
0.2
|
C4
|
A:CFQ1537
|
2.2
|
52.1
|
0.8
|
C1
|
A:CFQ1537
|
2.2
|
54.3
|
0.8
|
C3
|
A:CFQ1537
|
2.2
|
53.5
|
0.8
|
C2
|
A:CFQ1537
|
2.3
|
51.7
|
0.8
|
C1
|
A:CFQ1537
|
2.3
|
48.5
|
0.2
|
O1
|
A:CFQ1537
|
2.9
|
52.9
|
0.8
|
C5
|
A:CFQ1537
|
3.1
|
51.9
|
0.8
|
C2
|
A:CFQ1537
|
3.3
|
48.6
|
0.2
|
C6
|
A:CFQ1537
|
3.4
|
41.8
|
0.2
|
C3
|
A:CFQ1537
|
3.6
|
48.9
|
0.2
|
F2
|
A:CFQ1537
|
3.7
|
42.4
|
0.2
|
C14
|
A:CFQ1537
|
3.9
|
41.7
|
0.2
|
F3
|
A:CFQ1537
|
4.0
|
41.0
|
0.2
|
F2
|
A:CFQ1537
|
4.1
|
48.1
|
0.8
|
C6
|
A:CFQ1537
|
4.3
|
51.5
|
0.8
|
C7
|
A:CFQ1537
|
4.5
|
40.7
|
0.2
|
CG
|
A:TRP279
|
4.6
|
37.6
|
0.8
|
CD2
|
A:TRP279
|
4.6
|
39.5
|
0.8
|
C14
|
A:CFQ1537
|
4.6
|
49.1
|
0.8
|
CE3
|
A:TRP279
|
4.7
|
41.9
|
0.2
|
CD1
|
A:TRP279
|
4.7
|
38.2
|
0.8
|
C12
|
A:CFQ1537
|
4.7
|
40.0
|
0.2
|
CE2
|
A:TRP279
|
4.8
|
39.5
|
0.8
|
NE1
|
A:TRP279
|
4.8
|
37.4
|
0.8
|
CD2
|
A:TRP279
|
4.8
|
42.1
|
0.2
|
F3
|
A:CFQ1537
|
4.9
|
47.2
|
0.8
|
CB
|
A:TRP279
|
4.9
|
36.4
|
0.8
|
C7
|
A:CFQ1537
|
5.0
|
55.5
|
0.8
|
|
Arsenic binding site 2 out
of 8 in 2v98
Go back to
Arsenic Binding Sites List in 2v98
Arsenic binding site 2 out
of 8 in the Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place
Mono view
Stereo pair view
|
A full contact list of Arsenic with other atoms in the As binding
site number 2 of Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:As1537
b:50.1
occ:0.20
|
AS
|
A:CFQ1537
|
0.0
|
50.1
|
0.2
|
C3
|
A:CFQ1537
|
1.4
|
53.5
|
0.8
|
AS
|
A:CFQ1537
|
1.7
|
52.6
|
0.8
|
C3
|
A:CFQ1537
|
2.2
|
48.9
|
0.2
|
C4
|
A:CFQ1537
|
2.2
|
47.1
|
0.2
|
C1
|
A:CFQ1537
|
2.2
|
48.5
|
0.2
|
C2
|
A:CFQ1537
|
2.2
|
48.6
|
0.2
|
C2
|
A:CFQ1537
|
2.6
|
51.7
|
0.8
|
C4
|
A:CFQ1537
|
2.9
|
52.1
|
0.8
|
O1
|
A:CFQ1537
|
3.2
|
43.4
|
0.2
|
C5
|
A:CFQ1537
|
3.2
|
45.3
|
0.2
|
CD1
|
A:TRP279
|
3.2
|
38.2
|
0.8
|
CG
|
A:TRP279
|
3.4
|
37.6
|
0.8
|
NE1
|
A:TRP279
|
3.6
|
37.4
|
0.8
|
C1
|
A:CFQ1537
|
3.8
|
54.3
|
0.8
|
CB
|
A:TRP279
|
3.8
|
36.4
|
0.8
|
CD2
|
A:TRP279
|
3.8
|
39.5
|
0.8
|
CE2
|
A:TRP279
|
4.0
|
39.5
|
0.8
|
CB
|
A:TRP279
|
4.1
|
41.6
|
0.2
|
C5
|
A:CFQ1537
|
4.2
|
51.9
|
0.8
|
O1
|
A:CFQ1537
|
4.2
|
52.9
|
0.8
|
CG
|
A:TRP279
|
4.2
|
42.0
|
0.2
|
OH
|
A:TYR70
|
4.5
|
36.0
|
0.8
|
F2
|
A:CFQ1537
|
4.5
|
42.4
|
0.2
|
CD2
|
A:TRP279
|
4.5
|
42.1
|
0.2
|
C6
|
A:CFQ1537
|
4.6
|
41.8
|
0.2
|
O
|
A:HOH2506
|
4.7
|
29.7
|
0.8
|
CE3
|
A:TRP279
|
4.7
|
41.7
|
0.8
|
CD1
|
A:TRP279
|
4.8
|
42.0
|
0.2
|
CE3
|
A:TRP279
|
4.8
|
41.9
|
0.2
|
CZ
|
A:TYR70
|
4.8
|
36.5
|
0.8
|
CE1
|
A:TYR70
|
4.9
|
37.9
|
0.8
|
CZ2
|
A:TRP279
|
4.9
|
40.4
|
0.8
|
O
|
A:HOH2507
|
4.9
|
35.6
|
0.2
|
|
Arsenic binding site 3 out
of 8 in 2v98
Go back to
Arsenic Binding Sites List in 2v98
Arsenic binding site 3 out
of 8 in the Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place
Mono view
Stereo pair view
|
A full contact list of Arsenic with other atoms in the As binding
site number 3 of Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:As1538
b:50.1
occ:0.80
|
AS
|
A:CFQ1538
|
0.0
|
50.1
|
0.8
|
AS
|
A:CFQ1538
|
1.0
|
50.1
|
0.2
|
C3
|
A:CFQ1538
|
1.4
|
49.8
|
0.2
|
C4
|
A:CFQ1538
|
2.2
|
50.4
|
0.8
|
C3
|
A:CFQ1538
|
2.2
|
51.5
|
0.8
|
C1
|
A:CFQ1538
|
2.2
|
50.7
|
0.8
|
C2
|
A:CFQ1538
|
2.2
|
49.6
|
0.8
|
C1
|
A:CFQ1538
|
2.5
|
49.3
|
0.2
|
C4
|
A:CFQ1538
|
2.6
|
49.1
|
0.2
|
O1
|
A:CFQ1538
|
3.0
|
47.2
|
0.2
|
C2
|
A:CFQ1538
|
3.0
|
49.7
|
0.2
|
C5
|
A:CFQ1538
|
3.0
|
47.9
|
0.2
|
C5
|
A:CFQ1538
|
3.1
|
48.0
|
0.8
|
O1
|
A:CFQ1538
|
3.2
|
48.5
|
0.8
|
O3
|
A:CFQ1538
|
3.6
|
47.6
|
0.2
|
F2
|
A:CFQ1538
|
3.9
|
53.9
|
0.8
|
OE1
|
A:GLU199
|
4.2
|
23.3
|
0.8
|
CD2
|
A:TRP84
|
4.2
|
40.0
|
0.8
|
OE1
|
A:GLU199
|
4.3
|
29.1
|
0.2
|
CE3
|
A:TRP84
|
4.3
|
40.5
|
0.8
|
C6
|
A:CFQ1538
|
4.3
|
47.9
|
0.2
|
CA
|
A:GLY118
|
4.4
|
29.0
|
0.2
|
C6
|
A:CFQ1538
|
4.4
|
52.4
|
0.8
|
F2
|
A:CFQ1538
|
4.4
|
48.3
|
0.2
|
OE2
|
A:GLU199
|
4.5
|
22.1
|
0.8
|
CE2
|
A:TRP84
|
4.5
|
40.3
|
0.8
|
CZ3
|
A:TRP84
|
4.6
|
39.5
|
0.8
|
N2
|
A:CFQ1538
|
4.6
|
47.6
|
0.2
|
O
|
A:GLY117
|
4.6
|
28.7
|
0.2
|
CD2
|
A:HIS440
|
4.6
|
27.8
|
0.8
|
CG
|
A:TRP84
|
4.7
|
39.5
|
0.8
|
C14
|
A:CFQ1538
|
4.7
|
53.8
|
0.8
|
C14
|
A:CFQ1538
|
4.7
|
48.0
|
0.2
|
F1
|
A:CFQ1538
|
4.8
|
48.2
|
0.2
|
CD2
|
A:HIS440
|
4.8
|
35.0
|
0.2
|
CZ2
|
A:TRP84
|
4.8
|
38.9
|
0.8
|
CD
|
A:GLU199
|
4.8
|
22.9
|
0.8
|
CH2
|
A:TRP84
|
4.8
|
37.1
|
0.8
|
O3
|
A:CFQ1538
|
4.9
|
50.6
|
0.8
|
O
|
A:HIS440
|
4.9
|
36.1
|
0.2
|
NE1
|
A:TRP84
|
5.0
|
42.1
|
0.8
|
CA
|
A:GLY118
|
5.0
|
28.8
|
0.8
|
NE2
|
A:HIS440
|
5.0
|
25.2
|
0.8
|
|
Arsenic binding site 4 out
of 8 in 2v98
Go back to
Arsenic Binding Sites List in 2v98
Arsenic binding site 4 out
of 8 in the Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place
Mono view
Stereo pair view
|
A full contact list of Arsenic with other atoms in the As binding
site number 4 of Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:As1538
b:50.1
occ:0.20
|
AS
|
A:CFQ1538
|
0.0
|
50.1
|
0.2
|
AS
|
A:CFQ1538
|
1.0
|
50.1
|
0.8
|
C4
|
A:CFQ1538
|
2.0
|
50.4
|
0.8
|
C2
|
A:CFQ1538
|
2.1
|
49.6
|
0.8
|
C3
|
A:CFQ1538
|
2.2
|
49.8
|
0.2
|
C4
|
A:CFQ1538
|
2.2
|
49.1
|
0.2
|
C1
|
A:CFQ1538
|
2.2
|
49.3
|
0.2
|
C2
|
A:CFQ1538
|
2.2
|
49.7
|
0.2
|
C1
|
A:CFQ1538
|
2.3
|
50.7
|
0.8
|
C5
|
A:CFQ1538
|
3.2
|
47.9
|
0.2
|
C3
|
A:CFQ1538
|
3.2
|
51.5
|
0.8
|
C5
|
A:CFQ1538
|
3.2
|
48.0
|
0.8
|
CD2
|
A:TRP84
|
3.4
|
40.0
|
0.8
|
O1
|
A:CFQ1538
|
3.4
|
47.2
|
0.2
|
CE2
|
A:TRP84
|
3.5
|
40.3
|
0.8
|
CE3
|
A:TRP84
|
3.5
|
40.5
|
0.8
|
O1
|
A:CFQ1538
|
3.6
|
48.5
|
0.8
|
CZ3
|
A:TRP84
|
3.8
|
39.5
|
0.8
|
CZ2
|
A:TRP84
|
3.8
|
38.9
|
0.8
|
CH2
|
A:TRP84
|
3.9
|
37.1
|
0.8
|
CG
|
A:TRP84
|
4.0
|
39.5
|
0.8
|
O3
|
A:CFQ1538
|
4.0
|
47.6
|
0.2
|
NE1
|
A:TRP84
|
4.1
|
42.1
|
0.8
|
CD1
|
A:TRP84
|
4.3
|
41.2
|
0.8
|
OE1
|
A:GLU199
|
4.5
|
29.1
|
0.2
|
CE2
|
A:TRP84
|
4.5
|
39.1
|
0.2
|
CD2
|
A:TRP84
|
4.5
|
38.7
|
0.2
|
OE1
|
A:GLU199
|
4.5
|
23.3
|
0.8
|
O
|
A:HIS440
|
4.6
|
36.1
|
0.2
|
CB
|
A:TRP84
|
4.7
|
39.1
|
0.8
|
F2
|
A:CFQ1538
|
4.7
|
53.9
|
0.8
|
O
|
A:HIS440
|
4.7
|
33.4
|
0.8
|
CA
|
A:GLY441
|
4.8
|
33.0
|
0.8
|
OE2
|
A:GLU199
|
4.8
|
22.1
|
0.8
|
NE1
|
A:TRP84
|
4.8
|
39.6
|
0.2
|
CZ2
|
A:TRP84
|
4.8
|
39.1
|
0.2
|
N2
|
A:CFQ1538
|
4.8
|
47.6
|
0.2
|
CE3
|
A:TRP84
|
4.8
|
38.8
|
0.2
|
CG
|
A:TRP84
|
4.9
|
38.8
|
0.2
|
C6
|
A:CFQ1538
|
4.9
|
47.9
|
0.2
|
C6
|
A:CFQ1538
|
4.9
|
52.4
|
0.8
|
CD1
|
A:TRP84
|
5.0
|
39.1
|
0.2
|
|
Arsenic binding site 5 out
of 8 in 2v98
Go back to
Arsenic Binding Sites List in 2v98
Arsenic binding site 5 out
of 8 in the Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place
Mono view
Stereo pair view
|
A full contact list of Arsenic with other atoms in the As binding
site number 5 of Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:As1536
b:66.1
occ:0.80
|
AS
|
B:CFQ1536
|
0.0
|
66.1
|
0.8
|
AS
|
B:CFQ1536
|
0.7
|
57.1
|
0.2
|
C2
|
B:CFQ1536
|
1.6
|
57.2
|
0.2
|
C4
|
B:CFQ1536
|
2.2
|
65.3
|
0.8
|
C2
|
B:CFQ1536
|
2.2
|
66.5
|
0.8
|
C1
|
B:CFQ1536
|
2.3
|
67.5
|
0.8
|
C3
|
B:CFQ1536
|
2.3
|
66.4
|
0.8
|
C3
|
B:CFQ1536
|
2.4
|
57.0
|
0.2
|
C1
|
B:CFQ1536
|
2.5
|
57.2
|
0.2
|
C4
|
B:CFQ1536
|
2.7
|
56.5
|
0.2
|
O1
|
B:CFQ1536
|
3.0
|
61.4
|
0.8
|
O1
|
B:CFQ1536
|
3.1
|
54.9
|
0.2
|
C5
|
B:CFQ1536
|
3.1
|
62.8
|
0.8
|
O
|
B:HOH2198
|
3.4
|
25.1
|
0.8
|
C5
|
B:CFQ1536
|
3.5
|
55.6
|
0.2
|
F2
|
B:CFQ1536
|
4.1
|
53.4
|
0.2
|
CG
|
B:TRP279
|
4.2
|
46.1
|
0.8
|
CD2
|
B:TRP279
|
4.4
|
47.5
|
0.8
|
C6
|
B:CFQ1536
|
4.4
|
60.8
|
0.8
|
C6
|
B:CFQ1536
|
4.4
|
54.3
|
0.2
|
CB
|
B:TRP279
|
4.4
|
43.6
|
0.8
|
C12
|
B:CFQ1536
|
4.5
|
61.0
|
0.8
|
CD1
|
B:TRP279
|
4.5
|
47.4
|
0.8
|
OH
|
B:TYR70
|
4.7
|
41.4
|
0.2
|
C14
|
B:CFQ1536
|
4.7
|
54.0
|
0.2
|
CE2
|
B:TRP279
|
4.7
|
48.5
|
0.8
|
NE1
|
B:TRP279
|
4.8
|
49.8
|
0.8
|
C12
|
B:CFQ1536
|
4.8
|
54.0
|
0.2
|
CE3
|
B:TRP279
|
4.8
|
49.1
|
0.8
|
C7
|
B:CFQ1536
|
4.8
|
60.7
|
0.8
|
CD2
|
B:TRP279
|
4.9
|
43.7
|
0.2
|
CG
|
B:TRP279
|
4.9
|
43.5
|
0.2
|
F3
|
B:CFQ1536
|
5.0
|
54.2
|
0.2
|
|
Arsenic binding site 6 out
of 8 in 2v98
Go back to
Arsenic Binding Sites List in 2v98
Arsenic binding site 6 out
of 8 in the Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place
Mono view
Stereo pair view
|
A full contact list of Arsenic with other atoms in the As binding
site number 6 of Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:As1536
b:57.1
occ:0.20
|
AS
|
B:CFQ1536
|
0.0
|
57.1
|
0.2
|
AS
|
B:CFQ1536
|
0.7
|
66.1
|
0.8
|
C4
|
B:CFQ1536
|
1.8
|
65.3
|
0.8
|
C1
|
B:CFQ1536
|
2.2
|
67.5
|
0.8
|
C4
|
B:CFQ1536
|
2.2
|
56.5
|
0.2
|
C1
|
B:CFQ1536
|
2.2
|
57.2
|
0.2
|
C3
|
B:CFQ1536
|
2.2
|
57.0
|
0.2
|
C2
|
B:CFQ1536
|
2.3
|
57.2
|
0.2
|
C3
|
B:CFQ1536
|
2.4
|
66.4
|
0.8
|
C5
|
B:CFQ1536
|
2.7
|
62.8
|
0.8
|
O1
|
B:CFQ1536
|
2.8
|
61.4
|
0.8
|
C2
|
B:CFQ1536
|
2.9
|
66.5
|
0.8
|
O1
|
B:CFQ1536
|
3.0
|
54.9
|
0.2
|
C5
|
B:CFQ1536
|
3.1
|
55.6
|
0.2
|
O
|
B:HOH2198
|
3.9
|
25.1
|
0.8
|
F2
|
B:CFQ1536
|
4.3
|
53.4
|
0.2
|
C6
|
B:CFQ1536
|
4.3
|
60.8
|
0.8
|
CG
|
B:TRP279
|
4.4
|
46.1
|
0.8
|
CB
|
B:TRP279
|
4.4
|
43.6
|
0.8
|
C6
|
B:CFQ1536
|
4.4
|
54.3
|
0.2
|
CD2
|
B:TRP279
|
4.5
|
47.5
|
0.8
|
C14
|
B:CFQ1536
|
4.7
|
54.0
|
0.2
|
C12
|
B:CFQ1536
|
4.8
|
61.0
|
0.8
|
F3
|
B:CFQ1536
|
4.8
|
59.3
|
0.8
|
CE3
|
B:TRP279
|
4.8
|
49.1
|
0.8
|
F3
|
B:CFQ1536
|
4.9
|
54.2
|
0.2
|
CD1
|
B:TRP279
|
4.9
|
47.4
|
0.8
|
C7
|
B:CFQ1536
|
4.9
|
60.7
|
0.8
|
C14
|
B:CFQ1536
|
4.9
|
60.5
|
0.8
|
CD2
|
B:TRP279
|
5.0
|
43.7
|
0.2
|
|
Arsenic binding site 7 out
of 8 in 2v98
Go back to
Arsenic Binding Sites List in 2v98
Arsenic binding site 7 out
of 8 in the Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place
Mono view
Stereo pair view
|
A full contact list of Arsenic with other atoms in the As binding
site number 7 of Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:As1537
b:55.5
occ:0.80
|
AS
|
B:CFQ1537
|
0.0
|
55.5
|
0.8
|
AS
|
B:CFQ1537
|
0.5
|
50.8
|
0.2
|
C1
|
B:CFQ1537
|
1.7
|
51.4
|
0.2
|
C4
|
B:CFQ1537
|
2.2
|
55.6
|
0.8
|
C2
|
B:CFQ1537
|
2.2
|
55.0
|
0.8
|
C1
|
B:CFQ1537
|
2.2
|
57.3
|
0.8
|
C3
|
B:CFQ1537
|
2.2
|
58.0
|
0.8
|
C4
|
B:CFQ1537
|
2.4
|
50.9
|
0.2
|
C3
|
B:CFQ1537
|
2.4
|
51.6
|
0.2
|
C2
|
B:CFQ1537
|
2.5
|
50.8
|
0.2
|
C5
|
B:CFQ1537
|
3.1
|
53.4
|
0.8
|
O1
|
B:CFQ1537
|
3.2
|
51.9
|
0.8
|
C5
|
B:CFQ1537
|
3.4
|
50.4
|
0.2
|
O1
|
B:CFQ1537
|
3.5
|
50.4
|
0.2
|
O3
|
B:CFQ1537
|
3.9
|
51.6
|
0.2
|
CD2
|
B:TRP84
|
4.2
|
39.7
|
0.2
|
CE3
|
B:TRP84
|
4.2
|
39.5
|
0.2
|
CE3
|
B:TRP84
|
4.3
|
40.7
|
0.8
|
CD2
|
B:TRP84
|
4.3
|
41.7
|
0.8
|
F1
|
B:CFQ1537
|
4.3
|
51.0
|
0.8
|
OE1
|
B:GLU199
|
4.3
|
25.6
|
0.8
|
CE2
|
B:TRP84
|
4.4
|
39.9
|
0.2
|
CZ3
|
B:TRP84
|
4.4
|
39.6
|
0.2
|
C6
|
B:CFQ1537
|
4.5
|
52.6
|
0.8
|
F1
|
B:CFQ1537
|
4.6
|
50.6
|
0.2
|
OE1
|
B:GLU199
|
4.6
|
26.0
|
0.2
|
CZ3
|
B:TRP84
|
4.6
|
40.5
|
0.8
|
CE2
|
B:TRP84
|
4.6
|
41.9
|
0.8
|
CZ2
|
B:TRP84
|
4.6
|
39.6
|
0.2
|
O
|
B:HOH2333
|
4.6
|
34.8
|
0.2
|
CH2
|
B:TRP84
|
4.6
|
39.8
|
0.2
|
CA
|
B:GLY118
|
4.6
|
25.9
|
0.8
|
CG
|
B:TRP84
|
4.7
|
39.8
|
0.2
|
O
|
B:HOH2235
|
4.7
|
20.4
|
0.2
|
CD2
|
B:HIS440
|
4.7
|
32.9
|
0.8
|
CG
|
B:TRP84
|
4.7
|
41.2
|
0.8
|
C6
|
B:CFQ1537
|
4.8
|
50.6
|
0.2
|
O3
|
B:CFQ1537
|
4.8
|
54.2
|
0.8
|
O
|
B:HOH2332
|
4.8
|
63.5
|
0.8
|
N
|
B:GLY118
|
4.8
|
24.8
|
0.8
|
CH2
|
B:TRP84
|
4.9
|
40.7
|
0.8
|
CA
|
B:GLY118
|
4.9
|
29.8
|
0.2
|
C14
|
B:CFQ1537
|
4.9
|
52.3
|
0.8
|
O
|
B:HOH2236
|
4.9
|
18.6
|
0.8
|
NE1
|
B:TRP84
|
4.9
|
40.1
|
0.2
|
CZ2
|
B:TRP84
|
4.9
|
40.9
|
0.8
|
F2
|
B:CFQ1537
|
4.9
|
50.8
|
0.2
|
O
|
B:HOH2357
|
4.9
|
50.0
|
0.2
|
O
|
B:HOH2356
|
5.0
|
38.8
|
0.8
|
N2
|
B:CFQ1537
|
5.0
|
51.3
|
0.2
|
C14
|
B:CFQ1537
|
5.0
|
50.6
|
0.2
|
|
Arsenic binding site 8 out
of 8 in 2v98
Go back to
Arsenic Binding Sites List in 2v98
Arsenic binding site 8 out
of 8 in the Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place
Mono view
Stereo pair view
|
A full contact list of Arsenic with other atoms in the As binding
site number 8 of Structure of the Complex of Tcache with 1-(2-Nitrophenyl)-2,2,2- Trifluoroethyl-Arsenocholine After A 9 Seconds Annealing to Room Temperature, During the First 5 Seconds of Which Laser Irradiation at 266NM Took Place within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:As1537
b:50.8
occ:0.20
|
AS
|
B:CFQ1537
|
0.0
|
50.8
|
0.2
|
AS
|
B:CFQ1537
|
0.5
|
55.5
|
0.8
|
C2
|
B:CFQ1537
|
2.0
|
55.0
|
0.8
|
C3
|
B:CFQ1537
|
2.1
|
58.0
|
0.8
|
C1
|
B:CFQ1537
|
2.2
|
51.4
|
0.2
|
C4
|
B:CFQ1537
|
2.2
|
55.6
|
0.8
|
C2
|
B:CFQ1537
|
2.2
|
50.8
|
0.2
|
C4
|
B:CFQ1537
|
2.2
|
50.9
|
0.2
|
C3
|
B:CFQ1537
|
2.2
|
51.6
|
0.2
|
C1
|
B:CFQ1537
|
2.7
|
57.3
|
0.8
|
C5
|
B:CFQ1537
|
3.1
|
53.4
|
0.8
|
C5
|
B:CFQ1537
|
3.2
|
50.4
|
0.2
|
O1
|
B:CFQ1537
|
3.3
|
51.9
|
0.8
|
O1
|
B:CFQ1537
|
3.5
|
50.4
|
0.2
|
OE1
|
B:GLU199
|
3.9
|
25.6
|
0.8
|
OE1
|
B:GLU199
|
4.1
|
26.0
|
0.2
|
O3
|
B:CFQ1537
|
4.3
|
51.6
|
0.2
|
CD2
|
B:HIS440
|
4.3
|
32.9
|
0.8
|
CD2
|
B:TRP84
|
4.5
|
39.7
|
0.2
|
CE3
|
B:TRP84
|
4.5
|
40.7
|
0.8
|
CE3
|
B:TRP84
|
4.5
|
39.5
|
0.2
|
C6
|
B:CFQ1537
|
4.5
|
52.6
|
0.8
|
CD2
|
B:TRP84
|
4.5
|
41.7
|
0.8
|
CE2
|
B:TRP84
|
4.6
|
39.9
|
0.2
|
CZ3
|
B:TRP84
|
4.6
|
39.6
|
0.2
|
F1
|
B:CFQ1537
|
4.6
|
51.0
|
0.8
|
CZ3
|
B:TRP84
|
4.6
|
40.5
|
0.8
|
ND1
|
B:HIS440
|
4.6
|
30.3
|
0.2
|
CH2
|
B:TRP84
|
4.7
|
39.8
|
0.2
|
CZ2
|
B:TRP84
|
4.7
|
39.6
|
0.2
|
NE2
|
B:HIS440
|
4.7
|
31.5
|
0.8
|
F1
|
B:CFQ1537
|
4.7
|
50.6
|
0.2
|
CE2
|
B:TRP84
|
4.7
|
41.9
|
0.8
|
CD
|
B:GLU199
|
4.8
|
23.3
|
0.8
|
OE2
|
B:GLU199
|
4.8
|
23.4
|
0.8
|
C6
|
B:CFQ1537
|
4.8
|
50.6
|
0.2
|
O
|
B:HOH2357
|
4.8
|
50.0
|
0.2
|
O
|
B:HIS440
|
4.8
|
31.5
|
0.2
|
CA
|
B:GLY441
|
4.8
|
30.7
|
0.2
|
O
|
B:HOH2356
|
4.8
|
38.8
|
0.8
|
O
|
B:HIS440
|
4.8
|
28.0
|
0.8
|
CH2
|
B:TRP84
|
4.8
|
40.7
|
0.8
|
CA
|
B:GLY118
|
4.8
|
25.9
|
0.8
|
F2
|
B:CFQ1537
|
4.9
|
50.8
|
0.2
|
CA
|
B:GLY441
|
4.9
|
24.3
|
0.8
|
CE1
|
B:HIS440
|
4.9
|
29.4
|
0.2
|
CB
|
B:SER200
|
4.9
|
19.6
|
0.8
|
N
|
B:GLY118
|
4.9
|
24.8
|
0.8
|
CZ2
|
B:TRP84
|
4.9
|
40.9
|
0.8
|
|
Reference:
J.-P.Colletier,
A.Royant,
A.Specht,
B.Sanson,
F.Nachon,
P.Masson,
G.Zaccai,
J.L.Sussman,
M.Goeldner,
I.Silman,
D.Bourgeois,
M.Weik.
Use of A 'Caged' Analog to Study Traffic of Choline Within Acetylcholinesterase By Kinetic Crystallography Acta Crystallogr.,Sect.D V. 63 1115 2007.
ISSN: ISSN 0907-4449
PubMed: 18007027
DOI: 10.1107/S0907444907044472
Page generated: Wed Jul 10 11:30:03 2024
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