Fluorine in PDB 1z5b: Topoisomerase VI-B, Adp ALF4- Bound Dimer Form
Enzymatic activity of Topoisomerase VI-B, Adp ALF4- Bound Dimer Form
All present enzymatic activity of Topoisomerase VI-B, Adp ALF4- Bound Dimer Form:
5.99.1.3;
Protein crystallography data
The structure of Topoisomerase VI-B, Adp ALF4- Bound Dimer Form, PDB code: 1z5b
was solved by
K.D.Corbett,
J.M.Berger,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
2.00
|
Space group
|
P 32 1 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
74.077,
74.077,
344.381,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
17.9 /
20.8
|
Other elements in 1z5b:
The structure of Topoisomerase VI-B, Adp ALF4- Bound Dimer Form also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Topoisomerase VI-B, Adp ALF4- Bound Dimer Form
(pdb code 1z5b). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 8 binding sites of Fluorine where determined in the
Topoisomerase VI-B, Adp ALF4- Bound Dimer Form, PDB code: 1z5b:
Jump to Fluorine binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Fluorine binding site 1 out
of 8 in 1z5b
Go back to
Fluorine Binding Sites List in 1z5b
Fluorine binding site 1 out
of 8 in the Topoisomerase VI-B, Adp ALF4- Bound Dimer Form
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 1 of Topoisomerase VI-B, Adp ALF4- Bound Dimer Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F3001
b:20.6
occ:1.00
|
F1
|
A:ALF3001
|
0.0
|
20.6
|
1.0
|
AL
|
A:ALF3001
|
1.8
|
19.4
|
1.0
|
MG
|
A:MG2001
|
2.0
|
20.1
|
1.0
|
F3
|
A:ALF3001
|
2.5
|
20.7
|
1.0
|
F4
|
A:ALF3001
|
2.6
|
18.7
|
1.0
|
O1A
|
A:ADP1001
|
2.6
|
18.6
|
1.0
|
O
|
A:HOH4002
|
2.7
|
14.1
|
1.0
|
O3B
|
A:ADP1001
|
2.8
|
15.9
|
1.0
|
O
|
A:HOH4038
|
2.8
|
20.8
|
1.0
|
O3A
|
A:ADP1001
|
2.9
|
17.7
|
1.0
|
N
|
A:GLY111
|
3.0
|
7.7
|
1.0
|
O1B
|
A:ADP1001
|
3.0
|
16.2
|
1.0
|
PB
|
A:ADP1001
|
3.0
|
18.1
|
1.0
|
PA
|
A:ADP1001
|
3.1
|
18.6
|
1.0
|
CA
|
A:GLY111
|
3.2
|
7.2
|
1.0
|
OE2
|
A:GLU38
|
3.4
|
9.5
|
1.0
|
O
|
A:HOH4136
|
3.5
|
28.3
|
1.0
|
F2
|
A:ALF3001
|
3.6
|
19.4
|
1.0
|
O2A
|
A:ADP1001
|
3.8
|
15.5
|
1.0
|
N
|
A:VAL112
|
4.0
|
7.5
|
1.0
|
C
|
A:GLY111
|
4.1
|
7.5
|
1.0
|
OD1
|
A:ASN42
|
4.1
|
6.0
|
1.0
|
C
|
A:LEU110
|
4.2
|
8.0
|
1.0
|
N
|
A:LEU110
|
4.2
|
7.0
|
1.0
|
CD
|
A:GLU38
|
4.5
|
10.3
|
1.0
|
O
|
A:HOH4137
|
4.5
|
26.4
|
1.0
|
O5'
|
A:ADP1001
|
4.6
|
19.9
|
1.0
|
O2B
|
A:ADP1001
|
4.6
|
15.2
|
1.0
|
O
|
A:HOH4006
|
4.7
|
16.9
|
1.0
|
ND2
|
A:ASN42
|
4.8
|
4.8
|
1.0
|
CA
|
A:LEU110
|
4.8
|
7.5
|
1.0
|
N
|
A:GLY109
|
4.9
|
6.7
|
1.0
|
CG
|
A:ASN42
|
4.9
|
6.3
|
1.0
|
NZ
|
A:LYS427
|
5.0
|
17.6
|
1.0
|
|
Fluorine binding site 2 out
of 8 in 1z5b
Go back to
Fluorine Binding Sites List in 1z5b
Fluorine binding site 2 out
of 8 in the Topoisomerase VI-B, Adp ALF4- Bound Dimer Form
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 2 of Topoisomerase VI-B, Adp ALF4- Bound Dimer Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F3001
b:19.4
occ:1.00
|
F2
|
A:ALF3001
|
0.0
|
19.4
|
1.0
|
AL
|
A:ALF3001
|
1.8
|
19.4
|
1.0
|
F4
|
A:ALF3001
|
2.5
|
18.7
|
1.0
|
F3
|
A:ALF3001
|
2.6
|
20.7
|
1.0
|
O3B
|
A:ADP1001
|
2.6
|
15.9
|
1.0
|
O
|
A:HOH4002
|
2.7
|
14.1
|
1.0
|
N
|
A:TYR108
|
2.8
|
7.0
|
1.0
|
N
|
A:MET107
|
2.8
|
7.4
|
1.0
|
NZ
|
A:LYS427
|
2.9
|
17.6
|
1.0
|
CD2
|
A:TYR108
|
3.5
|
7.4
|
1.0
|
CB
|
A:TYR108
|
3.6
|
7.3
|
1.0
|
F1
|
A:ALF3001
|
3.6
|
20.6
|
1.0
|
CA
|
A:GLY106
|
3.7
|
7.7
|
1.0
|
CA
|
A:MET107
|
3.7
|
7.2
|
1.0
|
C
|
A:MET107
|
3.7
|
7.2
|
1.0
|
CA
|
A:TYR108
|
3.7
|
7.2
|
1.0
|
C
|
A:GLY106
|
3.7
|
7.7
|
1.0
|
CG
|
A:TYR108
|
3.8
|
7.1
|
1.0
|
CG
|
A:MET107
|
3.8
|
6.2
|
1.0
|
CE
|
A:LYS427
|
3.9
|
15.8
|
1.0
|
PB
|
A:ADP1001
|
4.1
|
18.1
|
1.0
|
N
|
A:GLY109
|
4.1
|
6.7
|
1.0
|
O
|
A:HOH4006
|
4.3
|
16.9
|
1.0
|
CB
|
A:MET107
|
4.3
|
7.3
|
1.0
|
O
|
A:HOH4137
|
4.4
|
26.4
|
1.0
|
C
|
A:TYR108
|
4.4
|
6.9
|
1.0
|
CE2
|
A:TYR108
|
4.5
|
7.6
|
1.0
|
O1B
|
A:ADP1001
|
4.6
|
16.2
|
1.0
|
O
|
A:HOH4136
|
4.6
|
28.3
|
1.0
|
MG
|
A:MG2001
|
4.7
|
20.1
|
1.0
|
O
|
A:ARG105
|
4.8
|
7.6
|
1.0
|
O3A
|
A:ADP1001
|
4.9
|
17.7
|
1.0
|
O
|
A:MET107
|
4.9
|
7.4
|
1.0
|
O
|
A:GLY106
|
4.9
|
7.2
|
1.0
|
CD1
|
A:TYR108
|
4.9
|
6.4
|
1.0
|
N
|
A:GLY106
|
5.0
|
7.7
|
1.0
|
|
Fluorine binding site 3 out
of 8 in 1z5b
Go back to
Fluorine Binding Sites List in 1z5b
Fluorine binding site 3 out
of 8 in the Topoisomerase VI-B, Adp ALF4- Bound Dimer Form
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 3 of Topoisomerase VI-B, Adp ALF4- Bound Dimer Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F3001
b:20.7
occ:1.00
|
F3
|
A:ALF3001
|
0.0
|
20.7
|
1.0
|
AL
|
A:ALF3001
|
1.8
|
19.4
|
1.0
|
O
|
A:HOH4136
|
2.1
|
28.3
|
1.0
|
F1
|
A:ALF3001
|
2.5
|
20.6
|
1.0
|
F2
|
A:ALF3001
|
2.6
|
19.4
|
1.0
|
MG
|
A:MG2001
|
2.6
|
20.1
|
1.0
|
O
|
A:HOH4137
|
2.6
|
26.4
|
1.0
|
O
|
A:HOH4002
|
2.6
|
14.1
|
1.0
|
O3B
|
A:ADP1001
|
2.7
|
15.9
|
1.0
|
CA
|
A:GLY106
|
3.0
|
7.7
|
1.0
|
O1B
|
A:ADP1001
|
3.1
|
16.2
|
1.0
|
NZ
|
A:LYS427
|
3.2
|
17.6
|
1.0
|
O
|
A:HOH4038
|
3.4
|
20.8
|
1.0
|
PB
|
A:ADP1001
|
3.5
|
18.1
|
1.0
|
F4
|
A:ALF3001
|
3.6
|
18.7
|
1.0
|
OE2
|
A:GLU38
|
3.7
|
9.5
|
1.0
|
N
|
A:MET107
|
3.9
|
7.4
|
1.0
|
N
|
A:GLY106
|
3.9
|
7.7
|
1.0
|
C
|
A:GLY106
|
4.0
|
7.7
|
1.0
|
OD1
|
A:ASN42
|
4.2
|
6.0
|
1.0
|
O3A
|
A:ADP1001
|
4.4
|
17.7
|
1.0
|
O1A
|
A:ADP1001
|
4.5
|
18.6
|
1.0
|
O
|
A:ARG105
|
4.5
|
7.6
|
1.0
|
C
|
A:ARG105
|
4.6
|
7.4
|
1.0
|
CE
|
A:LYS427
|
4.6
|
15.8
|
1.0
|
NZ
|
A:LYS98
|
4.8
|
5.2
|
1.0
|
O2B
|
A:ADP1001
|
4.8
|
15.2
|
1.0
|
CD
|
A:GLU38
|
4.9
|
10.3
|
1.0
|
OE1
|
A:GLU41
|
5.0
|
10.8
|
1.0
|
|
Fluorine binding site 4 out
of 8 in 1z5b
Go back to
Fluorine Binding Sites List in 1z5b
Fluorine binding site 4 out
of 8 in the Topoisomerase VI-B, Adp ALF4- Bound Dimer Form
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 4 of Topoisomerase VI-B, Adp ALF4- Bound Dimer Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F3001
b:18.7
occ:1.00
|
F4
|
A:ALF3001
|
0.0
|
18.7
|
1.0
|
AL
|
A:ALF3001
|
1.8
|
19.4
|
1.0
|
F2
|
A:ALF3001
|
2.5
|
19.4
|
1.0
|
F1
|
A:ALF3001
|
2.6
|
20.6
|
1.0
|
N
|
A:LEU110
|
2.7
|
7.0
|
1.0
|
O
|
A:HOH4002
|
2.7
|
14.1
|
1.0
|
O3B
|
A:ADP1001
|
2.7
|
15.9
|
1.0
|
N
|
A:GLY111
|
2.7
|
7.7
|
1.0
|
N
|
A:GLY109
|
3.1
|
6.7
|
1.0
|
CB
|
A:TYR108
|
3.3
|
7.3
|
1.0
|
CA
|
A:LEU110
|
3.3
|
7.5
|
1.0
|
O
|
A:HOH4006
|
3.4
|
16.9
|
1.0
|
CB
|
A:LEU110
|
3.5
|
7.6
|
1.0
|
C
|
A:LEU110
|
3.5
|
8.0
|
1.0
|
F3
|
A:ALF3001
|
3.6
|
20.7
|
1.0
|
N
|
A:TYR108
|
3.6
|
7.0
|
1.0
|
O3A
|
A:ADP1001
|
3.6
|
17.7
|
1.0
|
C
|
A:TYR108
|
3.7
|
6.9
|
1.0
|
CA
|
A:TYR108
|
3.7
|
7.2
|
1.0
|
C
|
A:GLY109
|
3.7
|
6.8
|
1.0
|
CA
|
A:GLY111
|
3.7
|
7.2
|
1.0
|
PB
|
A:ADP1001
|
3.8
|
18.1
|
1.0
|
CA
|
A:GLY109
|
3.8
|
6.9
|
1.0
|
CD2
|
A:TYR108
|
4.2
|
7.4
|
1.0
|
CG
|
A:TYR108
|
4.2
|
7.1
|
1.0
|
MG
|
A:MG2001
|
4.4
|
20.1
|
1.0
|
PA
|
A:ADP1001
|
4.6
|
18.6
|
1.0
|
O1B
|
A:ADP1001
|
4.6
|
16.2
|
1.0
|
O
|
A:TYR108
|
4.6
|
7.0
|
1.0
|
CG
|
A:LEU110
|
4.7
|
9.2
|
1.0
|
O2A
|
A:ADP1001
|
4.7
|
15.5
|
1.0
|
O
|
A:LEU110
|
4.7
|
8.3
|
1.0
|
NZ
|
A:LYS427
|
4.8
|
17.6
|
1.0
|
O1A
|
A:ADP1001
|
4.8
|
18.6
|
1.0
|
N
|
A:MET107
|
4.8
|
7.4
|
1.0
|
OE2
|
A:GLU38
|
4.8
|
9.5
|
1.0
|
O
|
A:GLY109
|
4.9
|
5.6
|
1.0
|
C
|
A:MET107
|
4.9
|
7.2
|
1.0
|
O2B
|
A:ADP1001
|
4.9
|
15.2
|
1.0
|
|
Fluorine binding site 5 out
of 8 in 1z5b
Go back to
Fluorine Binding Sites List in 1z5b
Fluorine binding site 5 out
of 8 in the Topoisomerase VI-B, Adp ALF4- Bound Dimer Form
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 5 of Topoisomerase VI-B, Adp ALF4- Bound Dimer Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F3002
b:19.2
occ:1.00
|
F1
|
B:ALF3002
|
0.0
|
19.2
|
1.0
|
AL
|
B:ALF3002
|
1.8
|
21.2
|
1.0
|
F3
|
B:ALF3002
|
2.5
|
21.2
|
1.0
|
O3B
|
B:ADP1002
|
2.6
|
18.6
|
1.0
|
F4
|
B:ALF3002
|
2.6
|
20.9
|
1.0
|
N
|
B:LEU110
|
2.7
|
7.1
|
1.0
|
O
|
B:HOH3003
|
2.7
|
15.8
|
1.0
|
N
|
B:GLY111
|
2.8
|
7.1
|
1.0
|
N
|
B:GLY109
|
3.2
|
7.1
|
1.0
|
CB
|
B:TYR108
|
3.4
|
6.7
|
1.0
|
CA
|
B:LEU110
|
3.4
|
6.8
|
1.0
|
O
|
B:HOH3025
|
3.5
|
16.4
|
1.0
|
O3A
|
B:ADP1002
|
3.6
|
15.6
|
1.0
|
C
|
B:LEU110
|
3.6
|
6.8
|
1.0
|
F2
|
B:ALF3002
|
3.6
|
24.1
|
1.0
|
CB
|
B:LEU110
|
3.6
|
8.3
|
1.0
|
C
|
B:TYR108
|
3.7
|
7.0
|
1.0
|
PB
|
B:ADP1002
|
3.7
|
17.4
|
1.0
|
N
|
B:TYR108
|
3.7
|
6.7
|
1.0
|
CA
|
B:GLY111
|
3.7
|
7.4
|
1.0
|
C
|
B:GLY109
|
3.7
|
7.5
|
1.0
|
CA
|
B:TYR108
|
3.7
|
7.0
|
1.0
|
CA
|
B:GLY109
|
3.8
|
7.0
|
1.0
|
CD2
|
B:TYR108
|
4.3
|
8.5
|
1.0
|
CG
|
B:TYR108
|
4.3
|
8.1
|
1.0
|
MG
|
B:MG2002
|
4.4
|
18.4
|
1.0
|
PA
|
B:ADP1002
|
4.5
|
17.4
|
1.0
|
O1B
|
B:ADP1002
|
4.5
|
16.4
|
1.0
|
O
|
B:TYR108
|
4.6
|
7.2
|
1.0
|
O2A
|
B:ADP1002
|
4.6
|
16.0
|
1.0
|
O1A
|
B:ADP1002
|
4.7
|
17.9
|
1.0
|
CG
|
B:LEU110
|
4.7
|
8.5
|
1.0
|
O
|
B:LEU110
|
4.8
|
6.9
|
1.0
|
O2B
|
B:ADP1002
|
4.8
|
16.7
|
1.0
|
O
|
B:GLY109
|
4.9
|
6.6
|
1.0
|
N
|
B:MET107
|
4.9
|
7.3
|
1.0
|
OE2
|
B:GLU38
|
4.9
|
9.9
|
1.0
|
C
|
B:MET107
|
5.0
|
6.8
|
1.0
|
|
Fluorine binding site 6 out
of 8 in 1z5b
Go back to
Fluorine Binding Sites List in 1z5b
Fluorine binding site 6 out
of 8 in the Topoisomerase VI-B, Adp ALF4- Bound Dimer Form
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 6 of Topoisomerase VI-B, Adp ALF4- Bound Dimer Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F3002
b:24.1
occ:1.00
|
F2
|
B:ALF3002
|
0.0
|
24.1
|
1.0
|
AL
|
B:ALF3002
|
1.8
|
21.2
|
1.0
|
O
|
B:HOH3165
|
2.4
|
31.3
|
1.0
|
F4
|
B:ALF3002
|
2.5
|
20.9
|
1.0
|
F3
|
B:ALF3002
|
2.5
|
21.2
|
1.0
|
NZ
|
B:LYS427
|
2.7
|
23.3
|
1.0
|
O
|
B:HOH3089
|
2.7
|
27.3
|
1.0
|
O
|
B:HOH3003
|
2.7
|
15.8
|
1.0
|
O3B
|
B:ADP1002
|
2.7
|
18.6
|
1.0
|
CA
|
B:GLY106
|
2.8
|
7.7
|
1.0
|
MG
|
B:MG2002
|
3.1
|
18.4
|
1.0
|
O1B
|
B:ADP1002
|
3.3
|
16.4
|
1.0
|
CE
|
B:LYS427
|
3.5
|
19.6
|
1.0
|
F1
|
B:ALF3002
|
3.6
|
19.2
|
1.0
|
PB
|
B:ADP1002
|
3.6
|
17.4
|
1.0
|
N
|
B:MET107
|
3.7
|
7.3
|
1.0
|
C
|
B:GLY106
|
3.8
|
7.5
|
1.0
|
N
|
B:GLY106
|
3.9
|
8.0
|
1.0
|
O
|
B:HOH3008
|
3.9
|
15.3
|
1.0
|
OE2
|
B:GLU38
|
4.0
|
9.9
|
1.0
|
O
|
B:ARG105
|
4.2
|
8.7
|
1.0
|
C
|
B:ARG105
|
4.4
|
8.2
|
1.0
|
O3A
|
B:ADP1002
|
4.6
|
15.6
|
1.0
|
OD1
|
B:ASN42
|
4.6
|
7.4
|
1.0
|
O1A
|
B:ADP1002
|
4.7
|
17.9
|
1.0
|
O2B
|
B:ADP1002
|
4.8
|
16.7
|
1.0
|
N
|
B:TYR108
|
4.8
|
6.7
|
1.0
|
CD
|
B:LYS427
|
4.9
|
16.9
|
1.0
|
NZ
|
B:LYS98
|
4.9
|
9.3
|
1.0
|
O
|
B:GLY106
|
5.0
|
6.9
|
1.0
|
|
Fluorine binding site 7 out
of 8 in 1z5b
Go back to
Fluorine Binding Sites List in 1z5b
Fluorine binding site 7 out
of 8 in the Topoisomerase VI-B, Adp ALF4- Bound Dimer Form
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 7 of Topoisomerase VI-B, Adp ALF4- Bound Dimer Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F3002
b:21.2
occ:1.00
|
F3
|
B:ALF3002
|
0.0
|
21.2
|
1.0
|
AL
|
B:ALF3002
|
1.8
|
21.2
|
1.0
|
F2
|
B:ALF3002
|
2.5
|
24.1
|
1.0
|
F1
|
B:ALF3002
|
2.5
|
19.2
|
1.0
|
O3B
|
B:ADP1002
|
2.6
|
18.6
|
1.0
|
N
|
B:TYR108
|
2.7
|
6.7
|
1.0
|
O
|
B:HOH3003
|
2.8
|
15.8
|
1.0
|
N
|
B:MET107
|
2.9
|
7.3
|
1.0
|
NZ
|
B:LYS427
|
3.2
|
23.3
|
1.0
|
CE
|
B:LYS427
|
3.3
|
19.6
|
1.0
|
CD2
|
B:TYR108
|
3.4
|
8.5
|
1.0
|
CB
|
B:TYR108
|
3.4
|
6.7
|
1.0
|
CA
|
B:TYR108
|
3.5
|
7.0
|
1.0
|
F4
|
B:ALF3002
|
3.6
|
20.9
|
1.0
|
C
|
B:MET107
|
3.6
|
6.8
|
1.0
|
CG
|
B:TYR108
|
3.6
|
8.1
|
1.0
|
CA
|
B:MET107
|
3.6
|
6.9
|
1.0
|
CG
|
B:MET107
|
3.7
|
5.1
|
1.0
|
C
|
B:GLY106
|
3.8
|
7.5
|
1.0
|
CA
|
B:GLY106
|
3.9
|
7.7
|
1.0
|
N
|
B:GLY109
|
4.1
|
7.1
|
1.0
|
PB
|
B:ADP1002
|
4.2
|
17.4
|
1.0
|
CB
|
B:MET107
|
4.2
|
7.5
|
1.0
|
C
|
B:TYR108
|
4.3
|
7.0
|
1.0
|
CE2
|
B:TYR108
|
4.3
|
9.1
|
1.0
|
O
|
B:HOH3025
|
4.4
|
16.4
|
1.0
|
CD
|
B:LYS427
|
4.4
|
16.9
|
1.0
|
O
|
B:HOH3089
|
4.7
|
27.3
|
1.0
|
O1B
|
B:ADP1002
|
4.7
|
16.4
|
1.0
|
CD1
|
B:TYR108
|
4.7
|
6.9
|
1.0
|
O
|
B:MET107
|
4.8
|
6.9
|
1.0
|
O3A
|
B:ADP1002
|
4.9
|
15.6
|
1.0
|
O
|
B:HOH3165
|
4.9
|
31.3
|
1.0
|
O
|
B:GLY106
|
5.0
|
6.9
|
1.0
|
MG
|
B:MG2002
|
5.0
|
18.4
|
1.0
|
O
|
B:ARG105
|
5.0
|
8.7
|
1.0
|
N
|
B:LEU110
|
5.0
|
7.1
|
1.0
|
|
Fluorine binding site 8 out
of 8 in 1z5b
Go back to
Fluorine Binding Sites List in 1z5b
Fluorine binding site 8 out
of 8 in the Topoisomerase VI-B, Adp ALF4- Bound Dimer Form
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 8 of Topoisomerase VI-B, Adp ALF4- Bound Dimer Form within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F3002
b:20.9
occ:1.00
|
F4
|
B:ALF3002
|
0.0
|
20.9
|
1.0
|
AL
|
B:ALF3002
|
1.8
|
21.2
|
1.0
|
MG
|
B:MG2002
|
2.0
|
18.4
|
1.0
|
F2
|
B:ALF3002
|
2.5
|
24.1
|
1.0
|
F1
|
B:ALF3002
|
2.6
|
19.2
|
1.0
|
O3B
|
B:ADP1002
|
2.6
|
18.6
|
1.0
|
O
|
B:HOH3003
|
2.7
|
15.8
|
1.0
|
O1A
|
B:ADP1002
|
2.7
|
17.9
|
1.0
|
O
|
B:HOH3008
|
2.9
|
15.3
|
1.0
|
O1B
|
B:ADP1002
|
2.9
|
16.4
|
1.0
|
PB
|
B:ADP1002
|
2.9
|
17.4
|
1.0
|
O3A
|
B:ADP1002
|
3.0
|
15.6
|
1.0
|
O
|
B:HOH3165
|
3.2
|
31.3
|
1.0
|
N
|
B:GLY111
|
3.2
|
7.1
|
1.0
|
PA
|
B:ADP1002
|
3.3
|
17.4
|
1.0
|
CA
|
B:GLY111
|
3.4
|
7.4
|
1.0
|
OE2
|
B:GLU38
|
3.4
|
9.9
|
1.0
|
F3
|
B:ALF3002
|
3.6
|
21.2
|
1.0
|
O2A
|
B:ADP1002
|
4.0
|
16.0
|
1.0
|
OD1
|
B:ASN42
|
4.0
|
7.4
|
1.0
|
N
|
B:VAL112
|
4.2
|
7.2
|
1.0
|
O
|
B:HOH3089
|
4.2
|
27.3
|
1.0
|
C
|
B:GLY111
|
4.3
|
7.0
|
1.0
|
N
|
B:LEU110
|
4.4
|
7.1
|
1.0
|
C
|
B:LEU110
|
4.4
|
6.8
|
1.0
|
CD
|
B:GLU38
|
4.5
|
8.5
|
1.0
|
O2B
|
B:ADP1002
|
4.5
|
16.7
|
1.0
|
O5'
|
B:ADP1002
|
4.7
|
18.2
|
1.0
|
O
|
B:HOH3025
|
4.7
|
16.4
|
1.0
|
NZ
|
B:LYS427
|
4.8
|
23.3
|
1.0
|
CG
|
B:ASN42
|
4.9
|
7.7
|
1.0
|
ND2
|
B:ASN42
|
4.9
|
4.0
|
1.0
|
N
|
B:GLY109
|
4.9
|
7.1
|
1.0
|
CA
|
B:GLY106
|
5.0
|
7.7
|
1.0
|
|
Reference:
K.D.Corbett,
J.M.Berger.
Structural Dissection of Atp Turnover in the Prototypical Ghl Atpase Topovi. Structure V. 13 873 2005.
ISSN: ISSN 0969-2126
PubMed: 15939019
DOI: 10.1016/J.STR.2005.03.013
Page generated: Wed Jul 31 13:36:27 2024
|