Fluorine in PDB 1nf0: Triosephosphate Isomerase in Complex with Dhap
Enzymatic activity of Triosephosphate Isomerase in Complex with Dhap
All present enzymatic activity of Triosephosphate Isomerase in Complex with Dhap:
5.3.1.1;
Protein crystallography data
The structure of Triosephosphate Isomerase in Complex with Dhap, PDB code: 1nf0
was solved by
G.Jogl,
S.Rozovsky,
A.E.Mcdermott,
L.Tong,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
40.00 /
1.60
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
47.258,
62.170,
160.684,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
21.2 /
26.8
|
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Triosephosphate Isomerase in Complex with Dhap
(pdb code 1nf0). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the
Triosephosphate Isomerase in Complex with Dhap, PDB code: 1nf0:
Jump to Fluorine binding site number:
1;
2;
3;
Fluorine binding site 1 out
of 3 in 1nf0
Go back to
Fluorine Binding Sites List in 1nf0
Fluorine binding site 1 out
of 3 in the Triosephosphate Isomerase in Complex with Dhap
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 1 of Triosephosphate Isomerase in Complex with Dhap within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F168
b:0.9
occ:0.57
|
F
|
A:FTR168
|
0.0
|
0.9
|
0.6
|
CZ3
|
A:FTR168
|
1.3
|
13.1
|
0.6
|
CE3
|
A:FTR168
|
2.3
|
14.7
|
0.6
|
CH2
|
A:FTR168
|
2.4
|
23.8
|
0.6
|
CH2
|
A:FTR168
|
2.7
|
31.9
|
0.4
|
O
|
A:ALA175
|
3.0
|
19.4
|
0.6
|
C
|
A:ALA175
|
3.0
|
17.0
|
0.6
|
CZ2
|
A:FTR168
|
3.0
|
20.6
|
0.4
|
CZ3
|
A:FTR168
|
3.1
|
32.8
|
0.4
|
N
|
A:ALA176
|
3.2
|
16.6
|
0.6
|
CB
|
A:LEU174
|
3.3
|
17.0
|
0.6
|
CB
|
A:ALA169
|
3.5
|
18.7
|
0.6
|
N
|
A:ALA175
|
3.5
|
25.4
|
0.6
|
C
|
A:LEU174
|
3.6
|
23.8
|
0.6
|
CA
|
A:ALA176
|
3.6
|
19.5
|
0.6
|
CD2
|
A:FTR168
|
3.6
|
13.3
|
0.6
|
CZ2
|
A:FTR168
|
3.6
|
28.3
|
0.6
|
CE2
|
A:FTR168
|
3.7
|
19.7
|
0.4
|
CA
|
A:ALA175
|
3.7
|
18.2
|
0.6
|
F
|
A:FTR168
|
3.7
|
25.4
|
0.4
|
CA
|
A:ALA176
|
3.8
|
20.0
|
0.4
|
CE3
|
A:FTR168
|
3.8
|
28.4
|
0.4
|
CB
|
A:ALA176
|
4.0
|
21.0
|
0.6
|
O
|
A:LEU174
|
4.0
|
22.5
|
0.6
|
N
|
A:ALA176
|
4.0
|
19.3
|
0.4
|
CB
|
A:ALA176
|
4.0
|
27.9
|
0.4
|
CD2
|
A:FTR168
|
4.1
|
20.8
|
0.4
|
CA
|
A:LEU174
|
4.1
|
18.5
|
0.6
|
CE2
|
A:FTR168
|
4.1
|
19.9
|
0.6
|
O
|
A:ALA175
|
4.1
|
16.1
|
0.4
|
CD1
|
A:LEU174
|
4.2
|
12.1
|
0.6
|
CA
|
A:ALA169
|
4.2
|
17.6
|
0.6
|
C
|
A:ALA175
|
4.2
|
16.5
|
0.4
|
CG
|
A:LEU174
|
4.3
|
27.7
|
0.6
|
O
|
A:LEU174
|
4.5
|
31.2
|
0.4
|
N
|
A:ALA169
|
4.5
|
11.6
|
0.6
|
NE1
|
A:FTR168
|
4.7
|
11.2
|
0.4
|
O
|
A:FTR168
|
4.8
|
19.4
|
0.4
|
CG
|
A:FTR168
|
4.9
|
12.8
|
0.6
|
C
|
A:FTR168
|
5.0
|
16.9
|
0.6
|
|
Fluorine binding site 2 out
of 3 in 1nf0
Go back to
Fluorine Binding Sites List in 1nf0
Fluorine binding site 2 out
of 3 in the Triosephosphate Isomerase in Complex with Dhap
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 2 of Triosephosphate Isomerase in Complex with Dhap within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F168
b:25.4
occ:0.43
|
F
|
A:FTR168
|
0.0
|
25.4
|
0.4
|
CG
|
A:LEU174
|
1.1
|
27.7
|
0.6
|
CB
|
A:LEU174
|
1.1
|
17.0
|
0.6
|
CZ3
|
A:FTR168
|
1.3
|
32.8
|
0.4
|
CD1
|
A:LEU174
|
1.6
|
12.1
|
0.6
|
CE3
|
A:FTR168
|
2.3
|
28.4
|
0.4
|
CH2
|
A:FTR168
|
2.4
|
31.9
|
0.4
|
CD2
|
A:LEU174
|
2.5
|
20.8
|
0.6
|
CA
|
A:LEU174
|
2.6
|
18.5
|
0.6
|
N
|
A:LEU174
|
3.2
|
13.5
|
0.6
|
OG1
|
A:THR172
|
3.5
|
13.3
|
0.6
|
CD2
|
A:FTR168
|
3.6
|
20.8
|
0.4
|
O
|
A:FTR168
|
3.6
|
16.0
|
0.6
|
C
|
A:LEU174
|
3.6
|
23.8
|
0.6
|
CZ2
|
A:FTR168
|
3.7
|
20.6
|
0.4
|
F
|
A:FTR168
|
3.7
|
0.9
|
0.6
|
CE3
|
A:FTR168
|
3.9
|
14.7
|
0.6
|
CE2
|
A:FTR168
|
4.1
|
19.7
|
0.4
|
C
|
A:GLY173
|
4.1
|
16.7
|
0.6
|
CZ3
|
A:FTR168
|
4.3
|
13.1
|
0.6
|
O
|
A:LEU174
|
4.3
|
22.5
|
0.6
|
N
|
A:ALA175
|
4.3
|
25.4
|
0.6
|
O
|
A:GLY173
|
4.5
|
34.6
|
0.6
|
C
|
A:FTR168
|
4.5
|
16.9
|
0.6
|
CD1
|
A:LEU131
|
4.5
|
15.6
|
1.0
|
CB
|
A:THR172
|
4.6
|
17.6
|
0.6
|
CA
|
A:ALA169
|
4.6
|
17.6
|
0.6
|
O
|
A:FTR168
|
4.8
|
19.4
|
0.4
|
N
|
A:ALA169
|
4.9
|
11.6
|
0.6
|
CG
|
A:FTR168
|
4.9
|
9.3
|
0.4
|
O
|
A:THR172
|
4.9
|
6.5
|
0.6
|
|
Fluorine binding site 3 out
of 3 in 1nf0
Go back to
Fluorine Binding Sites List in 1nf0
Fluorine binding site 3 out
of 3 in the Triosephosphate Isomerase in Complex with Dhap
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 3 of Triosephosphate Isomerase in Complex with Dhap within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F168
b:35.3
occ:1.00
|
F
|
B:FTR168
|
0.0
|
35.3
|
1.0
|
CZ3
|
B:FTR168
|
1.3
|
27.9
|
1.0
|
CE3
|
B:FTR168
|
2.3
|
21.1
|
1.0
|
CH2
|
B:FTR168
|
2.4
|
27.1
|
1.0
|
O
|
B:HOH1348
|
2.8
|
56.8
|
1.0
|
O
|
B:HOH1332
|
2.8
|
84.9
|
1.0
|
O
|
B:LEU174
|
3.3
|
25.2
|
1.0
|
O
|
B:ALA175
|
3.6
|
26.3
|
1.0
|
CD2
|
B:FTR168
|
3.6
|
16.0
|
1.0
|
CZ2
|
B:FTR168
|
3.7
|
24.3
|
1.0
|
O
|
B:HOH1269
|
3.7
|
20.5
|
1.0
|
C
|
B:ALA175
|
3.8
|
21.3
|
1.0
|
N
|
B:ALA176
|
3.9
|
15.7
|
1.0
|
CE2
|
B:FTR168
|
4.1
|
13.0
|
1.0
|
CA
|
B:ALA176
|
4.2
|
24.9
|
1.0
|
C
|
B:LEU174
|
4.2
|
19.7
|
1.0
|
CB
|
B:ALA169
|
4.4
|
18.2
|
1.0
|
CA
|
B:ALA175
|
4.6
|
13.1
|
1.0
|
CB
|
B:LEU174
|
4.6
|
26.2
|
1.0
|
CA
|
B:ALA169
|
4.7
|
13.2
|
1.0
|
O
|
B:FTR168
|
4.8
|
14.6
|
1.0
|
N
|
B:ALA175
|
4.9
|
15.3
|
1.0
|
CG
|
B:FTR168
|
4.9
|
15.4
|
1.0
|
|
Reference:
G.Jogl,
S.Rozovsky,
A.E.Mcdermott,
L.Tong.
Optimal Alignment For Enzymatic Proton Transfer: Structure of the Michaelis Complex of Triosephosphate Isomerase at 1.2-A Resolution Proc.Natl.Acad.Sci.Usa V. 100 50 2003.
ISSN: ISSN 0027-8424
PubMed: 12509510
DOI: 10.1073/PNAS.0233793100
Page generated: Wed Jul 31 12:07:23 2024
|