Magnesium in PDB 1p7l: S-Adenosylmethionine Synthetase Complexed with Amppnp and Met.
Enzymatic activity of S-Adenosylmethionine Synthetase Complexed with Amppnp and Met.
All present enzymatic activity of S-Adenosylmethionine Synthetase Complexed with Amppnp and Met.:
2.5.1.6;
Protein crystallography data
The structure of S-Adenosylmethionine Synthetase Complexed with Amppnp and Met., PDB code: 1p7l
was solved by
F.Takusagawa,
J.Komoto,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
10.00 /
2.50
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
225.820,
69.130,
118.230,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
21.3 /
24.2
|
Other elements in 1p7l:
The structure of S-Adenosylmethionine Synthetase Complexed with Amppnp and Met. also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the S-Adenosylmethionine Synthetase Complexed with Amppnp and Met.
(pdb code 1p7l). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 8 binding sites of Magnesium where determined in the
S-Adenosylmethionine Synthetase Complexed with Amppnp and Met., PDB code: 1p7l:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Magnesium binding site 1 out
of 8 in 1p7l
Go back to
Magnesium Binding Sites List in 1p7l
Magnesium binding site 1 out
of 8 in the S-Adenosylmethionine Synthetase Complexed with Amppnp and Met.
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of S-Adenosylmethionine Synthetase Complexed with Amppnp and Met. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg387
b:22.3
occ:1.00
|
O1G
|
A:ANP384
|
2.4
|
18.6
|
1.0
|
O1A
|
A:ANP384
|
2.4
|
14.4
|
1.0
|
NZ
|
A:LYS245
|
3.6
|
4.6
|
1.0
|
PG
|
A:ANP384
|
3.6
|
17.4
|
1.0
|
OE2
|
A:GLU8
|
3.7
|
5.2
|
1.0
|
PA
|
A:ANP384
|
3.8
|
4.4
|
1.0
|
N3B
|
A:ANP384
|
3.9
|
11.0
|
1.0
|
NZ
|
A:LYS165
|
4.0
|
2.0
|
1.0
|
OE1
|
A:GLU8
|
4.2
|
2.0
|
1.0
|
O
|
B:GLN119
|
4.3
|
15.5
|
1.0
|
OD2
|
B:ASP271
|
4.3
|
11.9
|
1.0
|
O2A
|
A:ANP384
|
4.3
|
12.3
|
1.0
|
OD1
|
B:ASP271
|
4.4
|
8.1
|
1.0
|
CD
|
A:GLU8
|
4.4
|
2.0
|
1.0
|
O2G
|
A:ANP384
|
4.4
|
21.5
|
1.0
|
OD2
|
B:ASP118
|
4.4
|
29.1
|
1.0
|
CE
|
A:LYS245
|
4.6
|
2.0
|
1.0
|
O3A
|
A:ANP384
|
4.6
|
11.9
|
1.0
|
O3G
|
A:ANP384
|
4.7
|
21.0
|
1.0
|
O
|
B:GLY259
|
4.7
|
12.5
|
1.0
|
CG
|
B:ASP271
|
4.8
|
10.6
|
1.0
|
O5'
|
A:ANP384
|
5.0
|
12.3
|
1.0
|
PB
|
A:ANP384
|
5.0
|
4.8
|
1.0
|
|
Magnesium binding site 2 out
of 8 in 1p7l
Go back to
Magnesium Binding Sites List in 1p7l
Magnesium binding site 2 out
of 8 in the S-Adenosylmethionine Synthetase Complexed with Amppnp and Met.
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of S-Adenosylmethionine Synthetase Complexed with Amppnp and Met. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg388
b:15.6
occ:1.00
|
O2B
|
A:ANP384
|
2.2
|
18.2
|
1.0
|
OD2
|
A:ASP16
|
2.2
|
22.0
|
1.0
|
O2G
|
A:ANP384
|
2.4
|
21.5
|
1.0
|
O2A
|
A:ANP384
|
2.4
|
12.3
|
1.0
|
CG
|
A:ASP16
|
3.1
|
15.2
|
1.0
|
OD1
|
A:ASP16
|
3.2
|
20.9
|
1.0
|
PB
|
A:ANP384
|
3.3
|
4.8
|
1.0
|
PG
|
A:ANP384
|
3.3
|
17.4
|
1.0
|
N3B
|
A:ANP384
|
3.5
|
11.0
|
1.0
|
PA
|
A:ANP384
|
3.6
|
4.4
|
1.0
|
O3A
|
A:ANP384
|
3.7
|
11.9
|
1.0
|
NZ
|
A:LYS245
|
4.0
|
4.6
|
1.0
|
K
|
A:K386
|
4.0
|
2.0
|
1.0
|
NH2
|
A:ARG244
|
4.1
|
2.0
|
1.0
|
O3G
|
A:ANP384
|
4.3
|
21.0
|
1.0
|
O1G
|
A:ANP384
|
4.3
|
18.6
|
1.0
|
O
|
A:CYS239
|
4.4
|
5.8
|
1.0
|
OD2
|
A:ASP238
|
4.4
|
10.4
|
1.0
|
O1A
|
A:ANP384
|
4.4
|
14.4
|
1.0
|
CE1
|
A:HIS14
|
4.4
|
4.7
|
1.0
|
CB
|
A:ASP16
|
4.5
|
15.7
|
1.0
|
CZ
|
A:ARG244
|
4.5
|
8.1
|
1.0
|
CB
|
A:ARG244
|
4.5
|
6.3
|
1.0
|
O5'
|
A:ANP384
|
4.5
|
12.3
|
1.0
|
O1B
|
A:ANP384
|
4.6
|
17.3
|
1.0
|
NE
|
A:ARG244
|
4.6
|
14.1
|
1.0
|
OE2
|
B:GLU42
|
4.9
|
22.3
|
1.0
|
NE2
|
A:HIS14
|
4.9
|
7.7
|
1.0
|
O
|
A:ARG244
|
5.0
|
2.0
|
1.0
|
|
Magnesium binding site 3 out
of 8 in 1p7l
Go back to
Magnesium Binding Sites List in 1p7l
Magnesium binding site 3 out
of 8 in the S-Adenosylmethionine Synthetase Complexed with Amppnp and Met.
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of S-Adenosylmethionine Synthetase Complexed with Amppnp and Met. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg487
b:25.0
occ:1.00
|
O1G
|
B:ANP484
|
2.3
|
13.6
|
1.0
|
O1A
|
B:ANP484
|
2.4
|
9.4
|
1.0
|
NZ
|
B:LYS245
|
3.4
|
14.4
|
1.0
|
PG
|
B:ANP484
|
3.5
|
20.6
|
1.0
|
OE2
|
B:GLU8
|
3.7
|
13.4
|
1.0
|
PA
|
B:ANP484
|
3.8
|
2.0
|
1.0
|
N3B
|
B:ANP484
|
3.9
|
16.4
|
1.0
|
NZ
|
B:LYS165
|
4.1
|
2.0
|
1.0
|
O2G
|
B:ANP484
|
4.3
|
24.5
|
1.0
|
O2A
|
B:ANP484
|
4.3
|
3.4
|
1.0
|
OD1
|
A:ASP271
|
4.3
|
9.7
|
1.0
|
OD2
|
A:ASP271
|
4.3
|
15.6
|
1.0
|
OE1
|
B:GLU8
|
4.4
|
2.0
|
1.0
|
O
|
A:GLN119
|
4.4
|
15.3
|
1.0
|
CD
|
B:GLU8
|
4.5
|
4.5
|
1.0
|
CE
|
B:LYS245
|
4.5
|
3.9
|
1.0
|
OD2
|
A:ASP118
|
4.5
|
2.0
|
1.0
|
O3G
|
B:ANP484
|
4.6
|
22.5
|
1.0
|
O
|
A:GLY259
|
4.6
|
19.3
|
1.0
|
O3A
|
B:ANP484
|
4.6
|
9.2
|
1.0
|
CG
|
A:ASP271
|
4.7
|
15.7
|
1.0
|
PB
|
B:ANP484
|
4.9
|
2.0
|
1.0
|
O5'
|
B:ANP484
|
5.0
|
24.6
|
1.0
|
CA
|
A:GLY260
|
5.0
|
2.4
|
1.0
|
|
Magnesium binding site 4 out
of 8 in 1p7l
Go back to
Magnesium Binding Sites List in 1p7l
Magnesium binding site 4 out
of 8 in the S-Adenosylmethionine Synthetase Complexed with Amppnp and Met.
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of S-Adenosylmethionine Synthetase Complexed with Amppnp and Met. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg488
b:10.1
occ:1.00
|
O2B
|
B:ANP484
|
2.3
|
19.9
|
1.0
|
OD2
|
B:ASP16
|
2.3
|
15.6
|
1.0
|
O2G
|
B:ANP484
|
2.4
|
24.5
|
1.0
|
O2A
|
B:ANP484
|
2.5
|
3.4
|
1.0
|
CG
|
B:ASP16
|
3.1
|
9.2
|
1.0
|
OD1
|
B:ASP16
|
3.2
|
14.1
|
1.0
|
PB
|
B:ANP484
|
3.3
|
2.0
|
1.0
|
PG
|
B:ANP484
|
3.4
|
20.6
|
1.0
|
N3B
|
B:ANP484
|
3.6
|
16.4
|
1.0
|
PA
|
B:ANP484
|
3.8
|
2.0
|
1.0
|
O3A
|
B:ANP484
|
3.8
|
9.2
|
1.0
|
NH2
|
B:ARG244
|
4.0
|
4.4
|
1.0
|
K
|
B:K486
|
4.1
|
2.0
|
1.0
|
NZ
|
B:LYS245
|
4.2
|
14.4
|
1.0
|
O3G
|
B:ANP484
|
4.3
|
22.5
|
1.0
|
O
|
B:CYS239
|
4.3
|
14.2
|
1.0
|
CZ
|
B:ARG244
|
4.4
|
5.2
|
1.0
|
O1G
|
B:ANP484
|
4.4
|
13.6
|
1.0
|
OD2
|
B:ASP238
|
4.4
|
12.1
|
1.0
|
CB
|
B:ASP16
|
4.5
|
11.2
|
1.0
|
CB
|
B:ARG244
|
4.5
|
8.0
|
1.0
|
CE1
|
B:HIS14
|
4.5
|
8.2
|
1.0
|
NE
|
B:ARG244
|
4.5
|
12.4
|
1.0
|
O1A
|
B:ANP484
|
4.5
|
9.4
|
1.0
|
O1B
|
B:ANP484
|
4.6
|
17.3
|
1.0
|
O5'
|
B:ANP484
|
4.7
|
24.6
|
1.0
|
OE2
|
A:GLU42
|
4.8
|
9.6
|
1.0
|
O
|
B:ARG244
|
5.0
|
7.7
|
1.0
|
|
Magnesium binding site 5 out
of 8 in 1p7l
Go back to
Magnesium Binding Sites List in 1p7l
Magnesium binding site 5 out
of 8 in the S-Adenosylmethionine Synthetase Complexed with Amppnp and Met.
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of S-Adenosylmethionine Synthetase Complexed with Amppnp and Met. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg688
b:47.9
occ:1.00
|
OD2
|
C:ASP16
|
2.1
|
4.6
|
1.0
|
O2B
|
C:PPK684
|
2.2
|
27.2
|
1.0
|
O2A
|
C:PPK684
|
2.7
|
16.2
|
1.0
|
OD1
|
C:ASP16
|
2.8
|
5.2
|
1.0
|
CG
|
C:ASP16
|
2.8
|
3.3
|
1.0
|
O2G
|
C:PPK684
|
3.0
|
11.1
|
1.0
|
PB
|
C:PPK684
|
3.6
|
24.8
|
1.0
|
PG
|
C:PPK684
|
3.9
|
21.8
|
1.0
|
N3B
|
C:PPK684
|
3.9
|
18.8
|
1.0
|
K
|
C:K686
|
4.0
|
17.8
|
1.0
|
NH2
|
C:ARG244
|
4.0
|
23.1
|
1.0
|
PA
|
C:PPK684
|
4.0
|
16.4
|
1.0
|
O
|
C:CYS239
|
4.0
|
19.2
|
1.0
|
O3A
|
C:PPK684
|
4.1
|
19.4
|
1.0
|
CZ
|
C:ARG244
|
4.2
|
16.1
|
1.0
|
CB
|
C:ARG244
|
4.2
|
19.5
|
1.0
|
CB
|
C:ASP16
|
4.2
|
6.8
|
1.0
|
NE
|
C:ARG244
|
4.3
|
17.8
|
1.0
|
NZ
|
C:LYS245
|
4.5
|
32.4
|
1.0
|
OE2
|
D:GLU42
|
4.5
|
9.5
|
1.0
|
OD2
|
C:ASP238
|
4.5
|
5.6
|
1.0
|
CE1
|
C:HIS14
|
4.6
|
2.0
|
1.0
|
O1B
|
C:PPK684
|
4.7
|
14.5
|
1.0
|
O3G
|
C:PPK684
|
4.7
|
6.4
|
1.0
|
CG
|
C:ARG244
|
4.8
|
19.2
|
1.0
|
O1A
|
C:PPK684
|
4.9
|
29.3
|
1.0
|
NH1
|
C:ARG244
|
4.9
|
15.1
|
1.0
|
O4A
|
C:PPK684
|
5.0
|
19.2
|
1.0
|
|
Magnesium binding site 6 out
of 8 in 1p7l
Go back to
Magnesium Binding Sites List in 1p7l
Magnesium binding site 6 out
of 8 in the S-Adenosylmethionine Synthetase Complexed with Amppnp and Met.
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of S-Adenosylmethionine Synthetase Complexed with Amppnp and Met. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg887
b:38.2
occ:1.00
|
O1G
|
D:PPK884
|
2.4
|
20.7
|
1.0
|
O1A
|
D:PPK884
|
2.5
|
18.6
|
1.0
|
OD1
|
C:ASP271
|
3.0
|
11.2
|
1.0
|
OD2
|
C:ASP271
|
3.2
|
23.9
|
1.0
|
CG
|
C:ASP271
|
3.5
|
25.3
|
1.0
|
PG
|
D:PPK884
|
3.5
|
11.5
|
1.0
|
N3B
|
D:PPK884
|
3.7
|
8.6
|
1.0
|
PA
|
D:PPK884
|
3.8
|
17.8
|
1.0
|
O3A
|
D:PPK884
|
3.8
|
11.6
|
1.0
|
OD2
|
C:ASP118
|
3.8
|
16.9
|
1.0
|
O
|
C:GLN119
|
4.0
|
19.6
|
1.0
|
NZ
|
D:LYS165
|
4.1
|
17.8
|
1.0
|
PB
|
D:PPK884
|
4.4
|
5.8
|
1.0
|
O3G
|
D:PPK884
|
4.4
|
12.5
|
1.0
|
O2G
|
D:PPK884
|
4.5
|
2.8
|
1.0
|
CG
|
C:ASP118
|
4.6
|
17.3
|
1.0
|
O4A
|
D:PPK884
|
4.7
|
9.6
|
1.0
|
OE2
|
D:GLU8
|
4.7
|
22.6
|
1.0
|
CA
|
C:GLY260
|
4.8
|
18.6
|
1.0
|
O2A
|
D:PPK884
|
4.8
|
23.1
|
1.0
|
NZ
|
D:LYS245
|
4.8
|
22.9
|
1.0
|
CB
|
C:ASP271
|
5.0
|
21.6
|
1.0
|
|
Magnesium binding site 7 out
of 8 in 1p7l
Go back to
Magnesium Binding Sites List in 1p7l
Magnesium binding site 7 out
of 8 in the S-Adenosylmethionine Synthetase Complexed with Amppnp and Met.
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 7 of S-Adenosylmethionine Synthetase Complexed with Amppnp and Met. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg687
b:19.8
occ:1.00
|
O1A
|
C:PPK684
|
2.4
|
29.3
|
1.0
|
O1G
|
C:PPK684
|
2.5
|
20.1
|
1.0
|
OD1
|
D:ASP271
|
3.2
|
18.5
|
1.0
|
OD2
|
D:ASP271
|
3.3
|
13.9
|
1.0
|
PA
|
C:PPK684
|
3.7
|
16.4
|
1.0
|
OD2
|
D:ASP118
|
3.7
|
20.6
|
1.0
|
CG
|
D:ASP271
|
3.7
|
20.6
|
1.0
|
PG
|
C:PPK684
|
3.7
|
21.8
|
1.0
|
O
|
D:GLN119
|
3.7
|
8.5
|
1.0
|
O3A
|
C:PPK684
|
3.9
|
19.4
|
1.0
|
NZ
|
C:LYS165
|
3.9
|
23.1
|
1.0
|
N3B
|
C:PPK684
|
3.9
|
18.8
|
1.0
|
O4A
|
C:PPK684
|
4.5
|
19.2
|
1.0
|
CG
|
D:ASP118
|
4.5
|
21.7
|
1.0
|
O2G
|
C:PPK684
|
4.5
|
11.1
|
1.0
|
PB
|
C:PPK684
|
4.5
|
24.8
|
1.0
|
OE2
|
C:GLU8
|
4.7
|
11.7
|
1.0
|
O2A
|
C:PPK684
|
4.7
|
16.2
|
1.0
|
NZ
|
C:LYS245
|
4.7
|
32.4
|
1.0
|
O3G
|
C:PPK684
|
4.7
|
6.4
|
1.0
|
OE1
|
C:GLU8
|
4.8
|
7.3
|
1.0
|
CA
|
D:GLY260
|
4.9
|
2.0
|
1.0
|
C
|
D:GLN119
|
4.9
|
3.8
|
1.0
|
CA
|
D:GLY120
|
4.9
|
2.0
|
1.0
|
CB
|
D:ASP118
|
5.0
|
14.2
|
1.0
|
|
Magnesium binding site 8 out
of 8 in 1p7l
Go back to
Magnesium Binding Sites List in 1p7l
Magnesium binding site 8 out
of 8 in the S-Adenosylmethionine Synthetase Complexed with Amppnp and Met.
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 8 of S-Adenosylmethionine Synthetase Complexed with Amppnp and Met. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg888
b:25.3
occ:1.00
|
O2B
|
D:PPK884
|
2.1
|
2.0
|
1.0
|
OD2
|
D:ASP16
|
2.1
|
7.4
|
1.0
|
O2A
|
D:PPK884
|
2.8
|
23.1
|
1.0
|
O2G
|
D:PPK884
|
2.8
|
2.8
|
1.0
|
CG
|
D:ASP16
|
2.8
|
5.5
|
1.0
|
OD1
|
D:ASP16
|
2.9
|
10.1
|
1.0
|
PB
|
D:PPK884
|
3.5
|
5.8
|
1.0
|
PG
|
D:PPK884
|
3.8
|
11.5
|
1.0
|
N3B
|
D:PPK884
|
3.8
|
8.6
|
1.0
|
NH2
|
D:ARG244
|
3.9
|
28.4
|
1.0
|
PA
|
D:PPK884
|
4.0
|
17.8
|
1.0
|
K
|
D:K886
|
4.0
|
42.0
|
1.0
|
O3A
|
D:PPK884
|
4.1
|
11.6
|
1.0
|
CB
|
D:ARG244
|
4.1
|
29.9
|
1.0
|
CZ
|
D:ARG244
|
4.2
|
27.2
|
1.0
|
O
|
D:CYS239
|
4.2
|
23.1
|
1.0
|
NE
|
D:ARG244
|
4.3
|
26.0
|
1.0
|
CB
|
D:ASP16
|
4.3
|
6.1
|
1.0
|
NZ
|
D:LYS245
|
4.3
|
22.9
|
1.0
|
OE2
|
C:GLU42
|
4.5
|
10.4
|
1.0
|
O3G
|
D:PPK884
|
4.6
|
12.5
|
1.0
|
CE1
|
D:HIS14
|
4.6
|
16.7
|
1.0
|
O1B
|
D:PPK884
|
4.6
|
2.0
|
1.0
|
OD2
|
D:ASP238
|
4.7
|
14.9
|
1.0
|
CG
|
D:ARG244
|
4.7
|
27.6
|
1.0
|
NH1
|
D:ARG244
|
4.8
|
16.9
|
1.0
|
O1A
|
D:PPK884
|
4.8
|
18.6
|
1.0
|
O1G
|
D:PPK884
|
4.9
|
20.7
|
1.0
|
O
|
D:ARG244
|
5.0
|
32.2
|
1.0
|
|
Reference:
J.Komoto,
T.Yamada,
Y.Takata,
G.D.Markham,
F.Takusagawa.
Crystal Structure of the S-Adenosylmethionine Synthetase Ternary Complex: A Novel Catalytic Mechanism of S-Adenosylmethionine Synthesis From Atp and Met. Biochemistry V. 43 1821 2004.
ISSN: ISSN 0006-2960
PubMed: 14967023
DOI: 10.1021/BI035611T
Page generated: Tue Aug 13 10:49:34 2024
|