Magnesium in PDB 4rxd: T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate
Protein crystallography data
The structure of T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate, PDB code: 4rxd
was solved by
R.Cao,
Y.-L.Liu,
E.Oldfield,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
29.55 /
2.00
|
|
Space group
|
C 1 2 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
156.340,
90.305,
88.709,
90.00,
89.91,
90.00
|
|
R / Rfree (%)
|
21.1 /
25.1
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate
(pdb code 4rxd). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 9 binding sites of Magnesium where determined in the
T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate, PDB code: 4rxd:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
Magnesium binding site 1 out
of 9 in 4rxd
Go back to
Magnesium Binding Sites List in 4rxd
Magnesium binding site 1 out
of 9 in the T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg1401
b:17.7
occ:1.00
|
OD2
|
A:ASP103
|
2.0
|
19.4
|
1.0
|
|
O12
|
A:RIS1404
|
2.1
|
16.8
|
1.0
|
|
O15
|
A:RIS1404
|
2.1
|
18.1
|
1.0
|
|
O
|
A:HOH1642
|
2.1
|
18.2
|
1.0
|
|
OD2
|
A:ASP107
|
2.1
|
16.8
|
1.0
|
|
O
|
A:HOH1653
|
2.2
|
20.8
|
1.0
|
|
CG
|
A:ASP103
|
3.0
|
18.4
|
1.0
|
|
MG
|
A:MG1403
|
3.0
|
16.4
|
1.0
|
|
CG
|
A:ASP107
|
3.2
|
18.6
|
1.0
|
|
OD1
|
A:ASP103
|
3.3
|
18.3
|
1.0
|
|
P14
|
A:RIS1404
|
3.3
|
18.4
|
1.0
|
|
P9
|
A:RIS1404
|
3.4
|
18.1
|
1.0
|
|
CB
|
A:ASP107
|
3.7
|
19.4
|
1.0
|
|
C8
|
A:RIS1404
|
3.7
|
17.9
|
1.0
|
|
O16
|
A:RIS1404
|
3.9
|
18.9
|
1.0
|
|
O
|
A:HOH1534
|
3.9
|
20.1
|
1.0
|
|
C7
|
A:RIS1404
|
3.9
|
18.2
|
1.0
|
|
O11
|
A:RIS1404
|
4.1
|
18.3
|
1.0
|
|
O
|
A:HOH1654
|
4.3
|
17.4
|
1.0
|
|
CB
|
A:ASP103
|
4.3
|
16.5
|
1.0
|
|
OD1
|
A:ASP107
|
4.3
|
16.6
|
1.0
|
|
O
|
A:ASP103
|
4.3
|
15.4
|
1.0
|
|
O
|
A:HOH1644
|
4.4
|
21.9
|
1.0
|
|
NH2
|
A:ARG112
|
4.4
|
21.9
|
1.0
|
|
OG
|
A:SER109
|
4.4
|
24.6
|
1.0
|
|
O
|
A:HOH1524
|
4.4
|
22.7
|
1.0
|
|
O17
|
A:RIS1404
|
4.5
|
19.2
|
1.0
|
|
O10
|
A:RIS1404
|
4.6
|
17.8
|
1.0
|
|
C
|
A:ASP103
|
4.6
|
16.8
|
1.0
|
|
OD1
|
A:ASP104
|
4.6
|
21.2
|
1.0
|
|
O
|
A:HOH1641
|
4.7
|
15.4
|
1.0
|
|
O
|
A:HOH1501
|
4.8
|
19.9
|
1.0
|
|
C2
|
A:RIS1404
|
4.9
|
17.3
|
1.0
|
|
O
|
A:HOH1545
|
4.9
|
20.7
|
1.0
|
|
MG
|
A:MG1402
|
4.9
|
22.8
|
1.0
|
|
O
|
A:HOH1518
|
5.0
|
24.6
|
1.0
|
|
Magnesium binding site 2 out
of 9 in 4rxd
Go back to
Magnesium Binding Sites List in 4rxd
Magnesium binding site 2 out
of 9 in the T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg1402
b:22.8
occ:1.00
|
O
|
A:HOH1644
|
2.0
|
21.9
|
1.0
|
|
O16
|
A:RIS1404
|
2.0
|
18.9
|
1.0
|
|
O11
|
A:RIS1404
|
2.1
|
18.3
|
1.0
|
|
OD2
|
A:ASP255
|
2.1
|
23.0
|
1.0
|
|
O
|
A:HOH1643
|
2.1
|
16.0
|
1.0
|
|
O
|
A:HOH1652
|
2.2
|
23.2
|
1.0
|
|
CG
|
A:ASP255
|
3.2
|
22.4
|
1.0
|
|
P9
|
A:RIS1404
|
3.3
|
18.1
|
1.0
|
|
P14
|
A:RIS1404
|
3.4
|
18.4
|
1.0
|
|
C8
|
A:RIS1404
|
3.6
|
17.9
|
1.0
|
|
OD1
|
A:ASP255
|
3.7
|
22.1
|
1.0
|
|
O13
|
A:RIS1404
|
3.7
|
19.7
|
1.0
|
|
O
|
A:HOH1545
|
3.8
|
20.7
|
1.0
|
|
OD1
|
A:ASP259
|
3.8
|
26.6
|
1.0
|
|
O12
|
A:RIS1404
|
4.1
|
16.8
|
1.0
|
|
O
|
A:HOH1653
|
4.1
|
20.8
|
1.0
|
|
OD1
|
A:ASP273
|
4.1
|
23.7
|
1.0
|
|
OD2
|
A:ASP273
|
4.2
|
24.0
|
1.0
|
|
O
|
A:ASP255
|
4.2
|
20.4
|
1.0
|
|
O15
|
A:RIS1404
|
4.3
|
18.1
|
1.0
|
|
NZ
|
A:LYS269
|
4.3
|
31.6
|
1.0
|
|
NE2
|
A:GLN252
|
4.3
|
19.1
|
1.0
|
|
CB
|
A:ASP255
|
4.4
|
21.2
|
1.0
|
|
CG
|
A:ASP259
|
4.4
|
28.7
|
1.0
|
|
O17
|
A:RIS1404
|
4.4
|
19.2
|
1.0
|
|
OD1
|
A:ASP256
|
4.5
|
22.6
|
1.0
|
|
O10
|
A:RIS1404
|
4.5
|
17.8
|
1.0
|
|
C
|
A:ASP255
|
4.5
|
21.1
|
1.0
|
|
CG
|
A:ASP273
|
4.6
|
24.2
|
1.0
|
|
O
|
A:HOH1647
|
4.6
|
47.6
|
1.0
|
|
CB
|
A:ASP259
|
4.7
|
28.6
|
1.0
|
|
CE
|
A:LYS269
|
4.8
|
31.0
|
1.0
|
|
O
|
A:HOH1534
|
4.8
|
20.1
|
1.0
|
|
MG
|
A:MG1401
|
4.9
|
17.7
|
1.0
|
|
N
|
A:ASP256
|
5.0
|
21.4
|
1.0
|
|
Magnesium binding site 3 out
of 9 in 4rxd
Go back to
Magnesium Binding Sites List in 4rxd
Magnesium binding site 3 out
of 9 in the T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg1403
b:16.4
occ:1.00
|
OD1
|
A:ASP103
|
2.0
|
18.3
|
1.0
|
|
O15
|
A:RIS1404
|
2.1
|
18.1
|
1.0
|
|
O
|
A:HOH1641
|
2.1
|
15.4
|
1.0
|
|
O
|
A:HOH1501
|
2.1
|
19.9
|
1.0
|
|
OD2
|
A:ASP107
|
2.1
|
16.8
|
1.0
|
|
O
|
A:HOH1654
|
2.1
|
17.4
|
1.0
|
|
CG
|
A:ASP103
|
3.0
|
18.4
|
1.0
|
|
CG
|
A:ASP107
|
3.0
|
18.6
|
1.0
|
|
MG
|
A:MG1401
|
3.0
|
17.7
|
1.0
|
|
OD2
|
A:ASP103
|
3.2
|
19.4
|
1.0
|
|
OD1
|
A:ASP107
|
3.2
|
16.6
|
1.0
|
|
P14
|
A:RIS1404
|
3.3
|
18.4
|
1.0
|
|
O17
|
A:RIS1404
|
3.5
|
19.2
|
1.0
|
|
OD1
|
A:ASP175
|
4.0
|
21.0
|
1.0
|
|
NZ
|
A:LYS278
|
4.1
|
31.4
|
1.0
|
|
O
|
A:HOH1653
|
4.2
|
20.8
|
1.0
|
|
OD2
|
A:ASP175
|
4.2
|
21.2
|
1.0
|
|
NE2
|
A:GLN172
|
4.2
|
16.4
|
1.0
|
|
O
|
A:HOH1545
|
4.3
|
20.7
|
1.0
|
|
O16
|
A:RIS1404
|
4.3
|
18.9
|
1.0
|
|
CG
|
A:ASP175
|
4.3
|
20.8
|
1.0
|
|
CB
|
A:ASP103
|
4.3
|
16.5
|
1.0
|
|
OE1
|
A:GLN172
|
4.3
|
18.7
|
1.0
|
|
CB
|
A:ASP107
|
4.4
|
19.4
|
1.0
|
|
C1
|
A:RIS1404
|
4.5
|
17.4
|
1.0
|
|
C8
|
A:RIS1404
|
4.6
|
17.9
|
1.0
|
|
C7
|
A:RIS1404
|
4.6
|
18.2
|
1.0
|
|
C2
|
A:RIS1404
|
4.6
|
17.3
|
1.0
|
|
NZ
|
A:LYS212
|
4.6
|
19.0
|
1.0
|
|
O12
|
A:RIS1404
|
4.6
|
16.8
|
1.0
|
|
CD
|
A:GLN172
|
4.7
|
17.2
|
1.0
|
|
O
|
A:HOH1642
|
4.8
|
18.2
|
1.0
|
|
O
|
A:ASP103
|
4.8
|
15.4
|
1.0
|
|
CA
|
A:ASP103
|
5.0
|
16.5
|
1.0
|
|
Magnesium binding site 4 out
of 9 in 4rxd
Go back to
Magnesium Binding Sites List in 4rxd
Magnesium binding site 4 out
of 9 in the T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg1501
b:17.7
occ:1.00
|
OD2
|
B:ASP103
|
2.0
|
19.7
|
1.0
|
|
O12
|
B:RIS1504
|
2.0
|
16.8
|
1.0
|
|
O
|
B:HOH1747
|
2.1
|
20.9
|
1.0
|
|
O
|
B:HOH1752
|
2.1
|
19.5
|
1.0
|
|
O15
|
B:RIS1504
|
2.1
|
16.4
|
1.0
|
|
OD2
|
B:ASP107
|
2.1
|
15.8
|
1.0
|
|
CG
|
B:ASP103
|
3.0
|
19.4
|
1.0
|
|
MG
|
B:MG1503
|
3.0
|
17.5
|
1.0
|
|
CG
|
B:ASP107
|
3.2
|
18.0
|
1.0
|
|
P14
|
B:RIS1504
|
3.3
|
17.7
|
1.0
|
|
P9
|
B:RIS1504
|
3.3
|
17.5
|
1.0
|
|
OD1
|
B:ASP103
|
3.4
|
19.1
|
1.0
|
|
C8
|
B:RIS1504
|
3.6
|
16.8
|
1.0
|
|
CB
|
B:ASP107
|
3.7
|
18.8
|
1.0
|
|
O16
|
B:RIS1504
|
3.9
|
18.5
|
1.0
|
|
C7
|
B:RIS1504
|
3.9
|
17.2
|
1.0
|
|
O
|
B:HOH1749
|
4.0
|
20.9
|
1.0
|
|
O11
|
B:RIS1504
|
4.1
|
18.7
|
1.0
|
|
O
|
B:HOH1624
|
4.2
|
17.8
|
1.0
|
|
OD1
|
B:ASP107
|
4.3
|
15.4
|
1.0
|
|
CB
|
B:ASP103
|
4.3
|
17.4
|
1.0
|
|
O
|
B:HOH1753
|
4.4
|
23.3
|
1.0
|
|
O
|
B:ASP103
|
4.4
|
16.8
|
1.0
|
|
OG
|
B:SER109
|
4.4
|
24.9
|
1.0
|
|
NH2
|
B:ARG112
|
4.4
|
21.0
|
1.0
|
|
O
|
B:HOH1631
|
4.4
|
21.5
|
1.0
|
|
O17
|
B:RIS1504
|
4.5
|
15.6
|
1.0
|
|
O10
|
B:RIS1504
|
4.5
|
18.5
|
1.0
|
|
C
|
B:ASP103
|
4.6
|
17.7
|
1.0
|
|
OD1
|
B:ASP104
|
4.7
|
21.4
|
1.0
|
|
O
|
B:HOH1746
|
4.7
|
16.6
|
1.0
|
|
O
|
B:HOH1751
|
4.8
|
19.5
|
1.0
|
|
C2
|
B:RIS1504
|
4.9
|
16.9
|
1.0
|
|
O
|
B:HOH1748
|
4.9
|
20.6
|
1.0
|
|
MG
|
B:MG1502
|
4.9
|
22.8
|
1.0
|
|
Magnesium binding site 5 out
of 9 in 4rxd
Go back to
Magnesium Binding Sites List in 4rxd
Magnesium binding site 5 out
of 9 in the T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg1502
b:22.8
occ:1.00
|
O
|
B:HOH1753
|
2.0
|
23.3
|
1.0
|
|
O16
|
B:RIS1504
|
2.1
|
18.5
|
1.0
|
|
OD2
|
B:ASP255
|
2.1
|
20.7
|
1.0
|
|
O
|
B:HOH1745
|
2.1
|
19.8
|
1.0
|
|
O11
|
B:RIS1504
|
2.1
|
18.7
|
1.0
|
|
O
|
B:HOH1604
|
2.1
|
15.6
|
1.0
|
|
CG
|
B:ASP255
|
3.1
|
21.7
|
1.0
|
|
P9
|
B:RIS1504
|
3.3
|
17.5
|
1.0
|
|
P14
|
B:RIS1504
|
3.4
|
17.7
|
1.0
|
|
O13
|
B:RIS1504
|
3.6
|
19.4
|
1.0
|
|
C8
|
B:RIS1504
|
3.6
|
16.8
|
1.0
|
|
OD1
|
B:ASP255
|
3.6
|
22.2
|
1.0
|
|
OD1
|
B:ASP259
|
3.7
|
27.2
|
1.0
|
|
O
|
B:HOH1748
|
3.8
|
20.6
|
1.0
|
|
O12
|
B:RIS1504
|
4.1
|
16.8
|
1.0
|
|
OD2
|
B:ASP273
|
4.1
|
25.5
|
1.0
|
|
O
|
B:ASP255
|
4.2
|
20.2
|
1.0
|
|
O
|
B:HOH1747
|
4.2
|
20.9
|
1.0
|
|
OD1
|
B:ASP273
|
4.2
|
23.8
|
1.0
|
|
O15
|
B:RIS1504
|
4.3
|
16.4
|
1.0
|
|
CG
|
B:ASP259
|
4.3
|
29.1
|
1.0
|
|
NZ
|
B:LYS269
|
4.3
|
29.1
|
1.0
|
|
CB
|
B:ASP255
|
4.3
|
20.6
|
1.0
|
|
NE2
|
B:GLN252
|
4.3
|
18.5
|
1.0
|
|
O17
|
B:RIS1504
|
4.4
|
15.6
|
1.0
|
|
O10
|
B:RIS1504
|
4.5
|
18.5
|
1.0
|
|
C
|
B:ASP255
|
4.5
|
20.9
|
1.0
|
|
OD1
|
B:ASP256
|
4.5
|
23.2
|
1.0
|
|
CG
|
B:ASP273
|
4.6
|
25.0
|
1.0
|
|
CE
|
B:LYS269
|
4.6
|
28.7
|
1.0
|
|
CB
|
B:ASP259
|
4.7
|
28.6
|
1.0
|
|
O
|
B:HOH1749
|
4.7
|
20.9
|
1.0
|
|
MG
|
B:MG1501
|
4.9
|
17.7
|
1.0
|
|
N
|
B:ASP256
|
5.0
|
21.2
|
1.0
|
|
CA
|
B:ASP255
|
5.0
|
21.1
|
1.0
|
|
Magnesium binding site 6 out
of 9 in 4rxd
Go back to
Magnesium Binding Sites List in 4rxd
Magnesium binding site 6 out
of 9 in the T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg1503
b:17.5
occ:1.00
|
O15
|
B:RIS1504
|
2.0
|
16.4
|
1.0
|
|
OD1
|
B:ASP103
|
2.0
|
19.1
|
1.0
|
|
O
|
B:HOH1746
|
2.1
|
16.6
|
1.0
|
|
OD2
|
B:ASP107
|
2.1
|
15.8
|
1.0
|
|
O
|
B:HOH1624
|
2.2
|
17.8
|
1.0
|
|
O
|
B:HOH1751
|
2.2
|
19.5
|
1.0
|
|
CG
|
B:ASP103
|
2.9
|
19.4
|
1.0
|
|
CG
|
B:ASP107
|
3.0
|
18.0
|
1.0
|
|
MG
|
B:MG1501
|
3.0
|
17.7
|
1.0
|
|
OD2
|
B:ASP103
|
3.1
|
19.7
|
1.0
|
|
OD1
|
B:ASP107
|
3.2
|
15.4
|
1.0
|
|
P14
|
B:RIS1504
|
3.3
|
17.7
|
1.0
|
|
O17
|
B:RIS1504
|
3.5
|
15.6
|
1.0
|
|
OD1
|
B:ASP175
|
4.0
|
19.6
|
1.0
|
|
O
|
B:HOH1747
|
4.1
|
20.9
|
1.0
|
|
OD2
|
B:ASP175
|
4.2
|
19.9
|
1.0
|
|
NZ
|
B:LYS278
|
4.2
|
30.4
|
1.0
|
|
NE2
|
B:GLN172
|
4.2
|
14.4
|
1.0
|
|
O16
|
B:RIS1504
|
4.3
|
18.5
|
1.0
|
|
OE1
|
B:GLN172
|
4.3
|
18.6
|
1.0
|
|
CG
|
B:ASP175
|
4.3
|
20.6
|
1.0
|
|
CB
|
B:ASP103
|
4.3
|
17.4
|
1.0
|
|
O
|
B:HOH1748
|
4.4
|
20.6
|
1.0
|
|
C1
|
B:RIS1504
|
4.4
|
17.2
|
1.0
|
|
CB
|
B:ASP107
|
4.4
|
18.8
|
1.0
|
|
C8
|
B:RIS1504
|
4.5
|
16.8
|
1.0
|
|
C7
|
B:RIS1504
|
4.5
|
17.2
|
1.0
|
|
C2
|
B:RIS1504
|
4.6
|
16.9
|
1.0
|
|
O12
|
B:RIS1504
|
4.6
|
16.8
|
1.0
|
|
NZ
|
B:LYS212
|
4.7
|
19.1
|
1.0
|
|
CD
|
B:GLN172
|
4.7
|
16.8
|
1.0
|
|
O
|
B:HOH1752
|
4.8
|
19.5
|
1.0
|
|
O
|
B:ASP103
|
4.8
|
16.8
|
1.0
|
|
CA
|
B:ASP103
|
4.9
|
17.1
|
1.0
|
|
Magnesium binding site 7 out
of 9 in 4rxd
Go back to
Magnesium Binding Sites List in 4rxd
Magnesium binding site 7 out
of 9 in the T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 7 of T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg1601
b:18.7
occ:1.00
|
OD2
|
C:ASP103
|
2.0
|
20.9
|
1.0
|
|
O
|
C:HOH1849
|
2.0
|
19.6
|
1.0
|
|
O12
|
C:RIS1600
|
2.1
|
18.4
|
1.0
|
|
O
|
C:HOH1842
|
2.1
|
22.4
|
1.0
|
|
OD2
|
C:ASP107
|
2.1
|
17.2
|
1.0
|
|
O15
|
C:RIS1600
|
2.1
|
17.3
|
1.0
|
|
CG
|
C:ASP103
|
3.0
|
19.7
|
1.0
|
|
MG
|
C:MG1603
|
3.1
|
16.6
|
1.0
|
|
CG
|
C:ASP107
|
3.2
|
19.9
|
1.0
|
|
P14
|
C:RIS1600
|
3.3
|
18.1
|
1.0
|
|
P9
|
C:RIS1600
|
3.3
|
18.5
|
1.0
|
|
OD1
|
C:ASP103
|
3.4
|
19.8
|
1.0
|
|
C8
|
C:RIS1600
|
3.6
|
17.8
|
1.0
|
|
CB
|
C:ASP107
|
3.7
|
19.7
|
1.0
|
|
O16
|
C:RIS1600
|
3.9
|
17.7
|
1.0
|
|
C7
|
C:RIS1600
|
3.9
|
19.1
|
1.0
|
|
O
|
C:HOH1845
|
3.9
|
22.3
|
1.0
|
|
O11
|
C:RIS1600
|
4.0
|
19.2
|
1.0
|
|
O
|
C:HOH1732
|
4.2
|
18.0
|
1.0
|
|
OD1
|
C:ASP107
|
4.3
|
17.6
|
1.0
|
|
CB
|
C:ASP103
|
4.3
|
17.9
|
1.0
|
|
OG
|
C:SER109
|
4.3
|
25.1
|
1.0
|
|
NH2
|
C:ARG112
|
4.3
|
21.6
|
1.0
|
|
O
|
C:HOH1715
|
4.4
|
20.9
|
1.0
|
|
O
|
C:ASP103
|
4.4
|
16.4
|
1.0
|
|
O
|
C:HOH1709
|
4.4
|
23.2
|
1.0
|
|
O10
|
C:RIS1600
|
4.5
|
19.3
|
1.0
|
|
O17
|
C:RIS1600
|
4.6
|
17.0
|
1.0
|
|
OD1
|
C:ASP104
|
4.6
|
21.3
|
1.0
|
|
C
|
C:ASP103
|
4.6
|
17.8
|
1.0
|
|
O
|
C:HOH1841
|
4.7
|
17.0
|
1.0
|
|
O
|
C:HOH1850
|
4.8
|
20.1
|
1.0
|
|
C2
|
C:RIS1600
|
4.9
|
17.9
|
1.0
|
|
MG
|
C:MG1602
|
4.9
|
22.0
|
1.0
|
|
O
|
C:HOH1844
|
5.0
|
20.6
|
1.0
|
|
O
|
C:HOH1744
|
5.0
|
24.7
|
1.0
|
|
Magnesium binding site 8 out
of 9 in 4rxd
Go back to
Magnesium Binding Sites List in 4rxd
Magnesium binding site 8 out
of 9 in the T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 8 of T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg1602
b:22.0
occ:1.00
|
O
|
C:HOH1715
|
2.0
|
20.9
|
1.0
|
|
O16
|
C:RIS1600
|
2.0
|
17.7
|
1.0
|
|
O11
|
C:RIS1600
|
2.1
|
19.2
|
1.0
|
|
O
|
C:HOH1843
|
2.1
|
18.6
|
1.0
|
|
OD2
|
C:ASP255
|
2.1
|
21.9
|
1.0
|
|
O
|
C:HOH1851
|
2.2
|
22.6
|
1.0
|
|
CG
|
C:ASP255
|
3.2
|
21.8
|
1.0
|
|
P9
|
C:RIS1600
|
3.3
|
18.5
|
1.0
|
|
P14
|
C:RIS1600
|
3.3
|
18.1
|
1.0
|
|
C8
|
C:RIS1600
|
3.6
|
17.8
|
1.0
|
|
O13
|
C:RIS1600
|
3.6
|
20.3
|
1.0
|
|
OD1
|
C:ASP255
|
3.7
|
21.9
|
1.0
|
|
O
|
C:HOH1844
|
3.7
|
20.6
|
1.0
|
|
OD1
|
C:ASP259
|
3.8
|
27.6
|
1.0
|
|
OD2
|
C:ASP273
|
4.1
|
24.4
|
1.0
|
|
O12
|
C:RIS1600
|
4.1
|
18.4
|
1.0
|
|
O
|
C:HOH1842
|
4.1
|
22.4
|
1.0
|
|
OD1
|
C:ASP273
|
4.1
|
22.9
|
1.0
|
|
O
|
C:ASP255
|
4.2
|
20.8
|
1.0
|
|
O15
|
C:RIS1600
|
4.3
|
17.3
|
1.0
|
|
NE2
|
C:GLN252
|
4.3
|
18.9
|
1.0
|
|
NZ
|
C:LYS269
|
4.4
|
28.7
|
1.0
|
|
CG
|
C:ASP259
|
4.4
|
29.2
|
1.0
|
|
CB
|
C:ASP255
|
4.4
|
20.7
|
1.0
|
|
O17
|
C:RIS1600
|
4.4
|
17.0
|
1.0
|
|
O10
|
C:RIS1600
|
4.5
|
19.3
|
1.0
|
|
OD1
|
C:ASP256
|
4.5
|
22.2
|
1.0
|
|
CG
|
C:ASP273
|
4.5
|
24.0
|
1.0
|
|
C
|
C:ASP255
|
4.5
|
20.9
|
1.0
|
|
CB
|
C:ASP259
|
4.7
|
28.5
|
1.0
|
|
CE
|
C:LYS269
|
4.7
|
28.6
|
1.0
|
|
O
|
C:HOH1845
|
4.7
|
22.3
|
1.0
|
|
MG
|
C:MG1601
|
4.9
|
18.7
|
1.0
|
|
Magnesium binding site 9 out
of 9 in 4rxd
Go back to
Magnesium Binding Sites List in 4rxd
Magnesium binding site 9 out
of 9 in the T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 9 of T. Brucei Farnesyl Diphosphate Synthase Complexed with Risedronate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg1603
b:16.6
occ:1.00
|
OD1
|
C:ASP103
|
2.0
|
19.8
|
1.0
|
|
O15
|
C:RIS1600
|
2.0
|
17.3
|
1.0
|
|
O
|
C:HOH1841
|
2.0
|
17.0
|
1.0
|
|
O
|
C:HOH1732
|
2.1
|
18.0
|
1.0
|
|
O
|
C:HOH1850
|
2.1
|
20.1
|
1.0
|
|
OD2
|
C:ASP107
|
2.1
|
17.2
|
1.0
|
|
CG
|
C:ASP103
|
2.9
|
19.7
|
1.0
|
|
CG
|
C:ASP107
|
3.0
|
19.9
|
1.0
|
|
MG
|
C:MG1601
|
3.1
|
18.7
|
1.0
|
|
OD2
|
C:ASP103
|
3.2
|
20.9
|
1.0
|
|
OD1
|
C:ASP107
|
3.2
|
17.6
|
1.0
|
|
P14
|
C:RIS1600
|
3.3
|
18.1
|
1.0
|
|
O17
|
C:RIS1600
|
3.5
|
17.0
|
1.0
|
|
OD1
|
C:ASP175
|
4.0
|
21.2
|
1.0
|
|
OD2
|
C:ASP175
|
4.2
|
20.7
|
1.0
|
|
O
|
C:HOH1842
|
4.2
|
22.4
|
1.0
|
|
OE1
|
C:GLN172
|
4.2
|
19.9
|
1.0
|
|
O16
|
C:RIS1600
|
4.3
|
17.7
|
1.0
|
|
NE2
|
C:GLN172
|
4.3
|
15.5
|
1.0
|
|
CG
|
C:ASP175
|
4.3
|
20.5
|
1.0
|
|
CB
|
C:ASP103
|
4.3
|
17.9
|
1.0
|
|
O
|
C:HOH1844
|
4.3
|
20.6
|
1.0
|
|
NZ
|
C:LYS278
|
4.4
|
31.2
|
1.0
|
|
C1
|
C:RIS1600
|
4.4
|
18.6
|
1.0
|
|
CB
|
C:ASP107
|
4.5
|
19.7
|
1.0
|
|
C8
|
C:RIS1600
|
4.5
|
17.8
|
1.0
|
|
C7
|
C:RIS1600
|
4.5
|
19.1
|
1.0
|
|
C2
|
C:RIS1600
|
4.6
|
17.9
|
1.0
|
|
NZ
|
C:LYS212
|
4.6
|
18.2
|
1.0
|
|
O12
|
C:RIS1600
|
4.7
|
18.4
|
1.0
|
|
CD
|
C:GLN172
|
4.7
|
17.2
|
1.0
|
|
O
|
C:HOH1849
|
4.7
|
19.6
|
1.0
|
|
O
|
C:ASP103
|
4.8
|
16.4
|
1.0
|
|
CA
|
C:ASP103
|
5.0
|
17.4
|
1.0
|
|
CE
|
C:LYS278
|
5.0
|
27.6
|
1.0
|
|
O
|
C:HOH1709
|
5.0
|
23.2
|
1.0
|
|
Reference:
Y.L.Liu,
R.Cao,
Y.Wang,
E.Oldfield.
Farnesyl Diphosphate Synthase Inhibitors with Unique Ligand-Binding Geometries. Acs Med Chem Lett V. 6 349 2015.
PubMed: 25815158
DOI: 10.1021/ML500528X
Page generated: Tue Aug 20 03:33:24 2024
|
