Manganese in PDB 2gls: Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution
Enzymatic activity of Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution
All present enzymatic activity of Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution:
6.3.1.2;
Protein crystallography data
The structure of Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution, PDB code: 2gls
was solved by
D.Eisenberg,
R.J.Almassy,
M.M.Yamashita,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
N/A /
3.50
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
235.500,
134.500,
200.100,
90.00,
102.80,
90.00
|
R / Rfree (%)
|
n/a /
n/a
|
Manganese Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
20;
Page 3, Binding sites: 21 -
24;
Binding sites:
The binding sites of Manganese atom in the Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution
(pdb code 2gls). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 24 binding sites of Manganese where determined in the
Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution, PDB code: 2gls:
Jump to Manganese binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Manganese binding site 1 out
of 24 in 2gls
Go back to
Manganese Binding Sites List in 2gls
Manganese binding site 1 out
of 24 in the Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn469
b:10.9
occ:1.00
|
O
|
A:HOH471
|
1.9
|
21.1
|
1.0
|
OE2
|
A:GLU212
|
1.9
|
9.0
|
1.0
|
OE1
|
A:GLU220
|
2.2
|
8.4
|
1.0
|
OE2
|
A:GLU131
|
2.3
|
5.7
|
1.0
|
CD
|
A:GLU212
|
2.7
|
9.0
|
1.0
|
CD
|
A:GLU220
|
2.8
|
8.4
|
1.0
|
OE2
|
A:GLU220
|
2.9
|
8.4
|
1.0
|
OE1
|
A:GLU212
|
3.3
|
9.0
|
1.0
|
CG
|
A:GLU212
|
3.5
|
9.0
|
1.0
|
CD
|
A:GLU131
|
3.5
|
5.7
|
1.0
|
O
|
A:HOH472
|
3.6
|
11.5
|
1.0
|
OE1
|
A:GLU131
|
4.1
|
5.7
|
1.0
|
CG
|
A:GLU220
|
4.2
|
8.4
|
1.0
|
CG
|
A:GLU131
|
4.5
|
5.7
|
1.0
|
CE1
|
A:HIS210
|
4.7
|
10.1
|
1.0
|
CB
|
A:GLU220
|
4.8
|
8.4
|
1.0
|
NE2
|
A:HIS210
|
4.9
|
10.1
|
1.0
|
CB
|
A:GLU212
|
5.0
|
9.0
|
1.0
|
OH
|
A:TYR179
|
5.0
|
17.4
|
1.0
|
|
Manganese binding site 2 out
of 24 in 2gls
Go back to
Manganese Binding Sites List in 2gls
Manganese binding site 2 out
of 24 in the Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn470
b:14.1
occ:1.00
|
OE2
|
A:GLU129
|
1.5
|
11.0
|
1.0
|
OE2
|
A:GLU357
|
1.9
|
8.5
|
1.0
|
ND1
|
A:HIS269
|
2.1
|
10.4
|
1.0
|
CE1
|
A:HIS269
|
2.7
|
10.4
|
1.0
|
CD
|
A:GLU129
|
2.8
|
11.0
|
1.0
|
O
|
A:HOH472
|
2.9
|
11.5
|
1.0
|
CD
|
A:GLU357
|
3.0
|
8.5
|
1.0
|
O
|
A:HOH473
|
3.2
|
18.2
|
1.0
|
OE1
|
A:GLU357
|
3.3
|
8.5
|
1.0
|
CG
|
A:HIS269
|
3.3
|
10.4
|
1.0
|
OE1
|
A:GLU129
|
3.4
|
11.0
|
1.0
|
CG
|
A:GLU129
|
3.8
|
11.0
|
1.0
|
NE2
|
A:HIS271
|
3.9
|
14.3
|
1.0
|
CB
|
A:HIS269
|
3.9
|
10.4
|
1.0
|
NE2
|
A:HIS269
|
3.9
|
10.4
|
1.0
|
CD2
|
A:HIS269
|
4.2
|
10.4
|
1.0
|
CG
|
A:GLU357
|
4.2
|
8.5
|
1.0
|
CE1
|
A:HIS271
|
4.4
|
14.3
|
1.0
|
CB
|
A:GLU129
|
4.8
|
11.0
|
1.0
|
O
|
A:HOH471
|
4.8
|
21.1
|
1.0
|
CD2
|
A:HIS271
|
4.8
|
14.3
|
1.0
|
NH1
|
A:ARG359
|
4.9
|
12.3
|
1.0
|
|
Manganese binding site 3 out
of 24 in 2gls
Go back to
Manganese Binding Sites List in 2gls
Manganese binding site 3 out
of 24 in the Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn469
b:10.9
occ:1.00
|
O
|
B:HOH471
|
1.9
|
21.1
|
1.0
|
OE2
|
B:GLU212
|
1.9
|
9.0
|
1.0
|
OE1
|
B:GLU220
|
2.2
|
8.4
|
1.0
|
OE2
|
B:GLU131
|
2.3
|
5.7
|
1.0
|
CD
|
B:GLU212
|
2.7
|
9.0
|
1.0
|
CD
|
B:GLU220
|
2.8
|
8.4
|
1.0
|
OE2
|
B:GLU220
|
2.9
|
8.4
|
1.0
|
OE1
|
B:GLU212
|
3.3
|
9.0
|
1.0
|
CG
|
B:GLU212
|
3.5
|
9.0
|
1.0
|
CD
|
B:GLU131
|
3.5
|
5.7
|
1.0
|
O
|
B:HOH472
|
3.6
|
11.5
|
1.0
|
OE1
|
B:GLU131
|
4.1
|
5.7
|
1.0
|
CG
|
B:GLU220
|
4.2
|
8.4
|
1.0
|
CG
|
B:GLU131
|
4.5
|
5.7
|
1.0
|
CE1
|
B:HIS210
|
4.7
|
10.1
|
1.0
|
CB
|
B:GLU220
|
4.8
|
8.4
|
1.0
|
NE2
|
B:HIS210
|
4.9
|
10.1
|
1.0
|
CB
|
B:GLU212
|
5.0
|
9.0
|
1.0
|
OH
|
B:TYR179
|
5.0
|
17.4
|
1.0
|
|
Manganese binding site 4 out
of 24 in 2gls
Go back to
Manganese Binding Sites List in 2gls
Manganese binding site 4 out
of 24 in the Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn470
b:14.1
occ:1.00
|
OE2
|
B:GLU129
|
1.5
|
11.0
|
1.0
|
OE2
|
B:GLU357
|
1.9
|
8.5
|
1.0
|
ND1
|
B:HIS269
|
2.1
|
10.4
|
1.0
|
CE1
|
B:HIS269
|
2.7
|
10.4
|
1.0
|
CD
|
B:GLU129
|
2.8
|
11.0
|
1.0
|
O
|
B:HOH472
|
2.9
|
11.5
|
1.0
|
CD
|
B:GLU357
|
3.0
|
8.5
|
1.0
|
O
|
B:HOH473
|
3.2
|
18.2
|
1.0
|
OE1
|
B:GLU357
|
3.3
|
8.5
|
1.0
|
CG
|
B:HIS269
|
3.3
|
10.4
|
1.0
|
OE1
|
B:GLU129
|
3.4
|
11.0
|
1.0
|
CG
|
B:GLU129
|
3.8
|
11.0
|
1.0
|
NE2
|
B:HIS271
|
3.9
|
14.3
|
1.0
|
CB
|
B:HIS269
|
3.9
|
10.4
|
1.0
|
NE2
|
B:HIS269
|
3.9
|
10.4
|
1.0
|
CD2
|
B:HIS269
|
4.2
|
10.4
|
1.0
|
CG
|
B:GLU357
|
4.2
|
8.5
|
1.0
|
CE1
|
B:HIS271
|
4.4
|
14.3
|
1.0
|
CB
|
B:GLU129
|
4.8
|
11.0
|
1.0
|
O
|
B:HOH471
|
4.8
|
21.1
|
1.0
|
CD2
|
B:HIS271
|
4.8
|
14.3
|
1.0
|
NH1
|
B:ARG359
|
4.9
|
12.3
|
1.0
|
|
Manganese binding site 5 out
of 24 in 2gls
Go back to
Manganese Binding Sites List in 2gls
Manganese binding site 5 out
of 24 in the Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 5 of Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn469
b:10.9
occ:1.00
|
O
|
C:HOH471
|
1.9
|
21.1
|
1.0
|
OE2
|
C:GLU212
|
1.9
|
9.0
|
1.0
|
OE1
|
C:GLU220
|
2.2
|
8.4
|
1.0
|
OE2
|
C:GLU131
|
2.3
|
5.7
|
1.0
|
CD
|
C:GLU212
|
2.7
|
9.0
|
1.0
|
CD
|
C:GLU220
|
2.8
|
8.4
|
1.0
|
OE2
|
C:GLU220
|
2.9
|
8.4
|
1.0
|
OE1
|
C:GLU212
|
3.3
|
9.0
|
1.0
|
CG
|
C:GLU212
|
3.5
|
9.0
|
1.0
|
CD
|
C:GLU131
|
3.5
|
5.7
|
1.0
|
O
|
C:HOH472
|
3.6
|
11.5
|
1.0
|
OE1
|
C:GLU131
|
4.1
|
5.7
|
1.0
|
CG
|
C:GLU220
|
4.2
|
8.4
|
1.0
|
CG
|
C:GLU131
|
4.5
|
5.7
|
1.0
|
CE1
|
C:HIS210
|
4.7
|
10.1
|
1.0
|
CB
|
C:GLU220
|
4.8
|
8.4
|
1.0
|
NE2
|
C:HIS210
|
4.9
|
10.1
|
1.0
|
CB
|
C:GLU212
|
5.0
|
9.0
|
1.0
|
OH
|
C:TYR179
|
5.0
|
17.4
|
1.0
|
|
Manganese binding site 6 out
of 24 in 2gls
Go back to
Manganese Binding Sites List in 2gls
Manganese binding site 6 out
of 24 in the Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 6 of Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn470
b:14.1
occ:1.00
|
OE2
|
C:GLU129
|
1.5
|
11.0
|
1.0
|
OE2
|
C:GLU357
|
1.9
|
8.5
|
1.0
|
ND1
|
C:HIS269
|
2.1
|
10.4
|
1.0
|
CE1
|
C:HIS269
|
2.7
|
10.4
|
1.0
|
CD
|
C:GLU129
|
2.8
|
11.0
|
1.0
|
O
|
C:HOH472
|
2.9
|
11.5
|
1.0
|
CD
|
C:GLU357
|
3.0
|
8.5
|
1.0
|
O
|
C:HOH473
|
3.2
|
18.2
|
1.0
|
OE1
|
C:GLU357
|
3.3
|
8.5
|
1.0
|
CG
|
C:HIS269
|
3.3
|
10.4
|
1.0
|
OE1
|
C:GLU129
|
3.4
|
11.0
|
1.0
|
CG
|
C:GLU129
|
3.8
|
11.0
|
1.0
|
NE2
|
C:HIS271
|
3.9
|
14.3
|
1.0
|
CB
|
C:HIS269
|
3.9
|
10.4
|
1.0
|
NE2
|
C:HIS269
|
3.9
|
10.4
|
1.0
|
CD2
|
C:HIS269
|
4.2
|
10.4
|
1.0
|
CG
|
C:GLU357
|
4.2
|
8.5
|
1.0
|
CE1
|
C:HIS271
|
4.4
|
14.3
|
1.0
|
CB
|
C:GLU129
|
4.8
|
11.0
|
1.0
|
O
|
C:HOH471
|
4.8
|
21.1
|
1.0
|
CD2
|
C:HIS271
|
4.8
|
14.3
|
1.0
|
NH1
|
C:ARG359
|
4.9
|
12.3
|
1.0
|
|
Manganese binding site 7 out
of 24 in 2gls
Go back to
Manganese Binding Sites List in 2gls
Manganese binding site 7 out
of 24 in the Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 7 of Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn469
b:10.9
occ:1.00
|
O
|
D:HOH471
|
1.9
|
21.1
|
1.0
|
OE2
|
D:GLU212
|
1.9
|
9.0
|
1.0
|
OE1
|
D:GLU220
|
2.2
|
8.4
|
1.0
|
OE2
|
D:GLU131
|
2.3
|
5.7
|
1.0
|
CD
|
D:GLU212
|
2.7
|
9.0
|
1.0
|
CD
|
D:GLU220
|
2.8
|
8.4
|
1.0
|
OE2
|
D:GLU220
|
2.9
|
8.4
|
1.0
|
OE1
|
D:GLU212
|
3.3
|
9.0
|
1.0
|
CG
|
D:GLU212
|
3.5
|
9.0
|
1.0
|
CD
|
D:GLU131
|
3.5
|
5.7
|
1.0
|
O
|
D:HOH472
|
3.6
|
11.5
|
1.0
|
OE1
|
D:GLU131
|
4.1
|
5.7
|
1.0
|
CG
|
D:GLU220
|
4.2
|
8.4
|
1.0
|
CG
|
D:GLU131
|
4.5
|
5.7
|
1.0
|
CE1
|
D:HIS210
|
4.7
|
10.1
|
1.0
|
CB
|
D:GLU220
|
4.8
|
8.4
|
1.0
|
NE2
|
D:HIS210
|
4.9
|
10.1
|
1.0
|
CB
|
D:GLU212
|
5.0
|
9.0
|
1.0
|
OH
|
D:TYR179
|
5.0
|
17.4
|
1.0
|
|
Manganese binding site 8 out
of 24 in 2gls
Go back to
Manganese Binding Sites List in 2gls
Manganese binding site 8 out
of 24 in the Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 8 of Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn470
b:14.1
occ:1.00
|
OE2
|
D:GLU129
|
1.5
|
11.0
|
1.0
|
OE2
|
D:GLU357
|
1.9
|
8.5
|
1.0
|
ND1
|
D:HIS269
|
2.1
|
10.4
|
1.0
|
CE1
|
D:HIS269
|
2.7
|
10.4
|
1.0
|
CD
|
D:GLU129
|
2.8
|
11.0
|
1.0
|
O
|
D:HOH472
|
2.9
|
11.5
|
1.0
|
CD
|
D:GLU357
|
3.0
|
8.5
|
1.0
|
O
|
D:HOH473
|
3.2
|
18.2
|
1.0
|
OE1
|
D:GLU357
|
3.3
|
8.5
|
1.0
|
CG
|
D:HIS269
|
3.3
|
10.4
|
1.0
|
OE1
|
D:GLU129
|
3.4
|
11.0
|
1.0
|
CG
|
D:GLU129
|
3.8
|
11.0
|
1.0
|
NE2
|
D:HIS271
|
3.9
|
14.3
|
1.0
|
CB
|
D:HIS269
|
3.9
|
10.4
|
1.0
|
NE2
|
D:HIS269
|
3.9
|
10.4
|
1.0
|
CD2
|
D:HIS269
|
4.2
|
10.4
|
1.0
|
CG
|
D:GLU357
|
4.2
|
8.5
|
1.0
|
CE1
|
D:HIS271
|
4.4
|
14.3
|
1.0
|
CB
|
D:GLU129
|
4.8
|
11.0
|
1.0
|
O
|
D:HOH471
|
4.8
|
21.1
|
1.0
|
CD2
|
D:HIS271
|
4.8
|
14.3
|
1.0
|
NH1
|
D:ARG359
|
4.9
|
12.3
|
1.0
|
|
Manganese binding site 9 out
of 24 in 2gls
Go back to
Manganese Binding Sites List in 2gls
Manganese binding site 9 out
of 24 in the Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 9 of Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mn469
b:10.9
occ:1.00
|
O
|
E:HOH471
|
1.9
|
21.1
|
1.0
|
OE2
|
E:GLU212
|
1.9
|
9.0
|
1.0
|
OE1
|
E:GLU220
|
2.2
|
8.4
|
1.0
|
OE2
|
E:GLU131
|
2.3
|
5.7
|
1.0
|
CD
|
E:GLU212
|
2.7
|
9.0
|
1.0
|
CD
|
E:GLU220
|
2.8
|
8.4
|
1.0
|
OE2
|
E:GLU220
|
2.9
|
8.4
|
1.0
|
OE1
|
E:GLU212
|
3.3
|
9.0
|
1.0
|
CG
|
E:GLU212
|
3.5
|
9.0
|
1.0
|
CD
|
E:GLU131
|
3.5
|
5.7
|
1.0
|
O
|
E:HOH472
|
3.6
|
11.5
|
1.0
|
OE1
|
E:GLU131
|
4.1
|
5.7
|
1.0
|
CG
|
E:GLU220
|
4.2
|
8.4
|
1.0
|
CG
|
E:GLU131
|
4.5
|
5.7
|
1.0
|
CE1
|
E:HIS210
|
4.7
|
10.1
|
1.0
|
CB
|
E:GLU220
|
4.8
|
8.4
|
1.0
|
NE2
|
E:HIS210
|
4.9
|
10.1
|
1.0
|
CB
|
E:GLU212
|
5.0
|
9.0
|
1.0
|
OH
|
E:TYR179
|
5.0
|
17.4
|
1.0
|
|
Manganese binding site 10 out
of 24 in 2gls
Go back to
Manganese Binding Sites List in 2gls
Manganese binding site 10 out
of 24 in the Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 10 of Refined Atomic Model of Glutamine Synthetase at 3.5 Angstroms Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mn470
b:14.1
occ:1.00
|
OE2
|
E:GLU129
|
1.5
|
11.0
|
1.0
|
OE2
|
E:GLU357
|
1.9
|
8.5
|
1.0
|
ND1
|
E:HIS269
|
2.1
|
10.4
|
1.0
|
CE1
|
E:HIS269
|
2.7
|
10.4
|
1.0
|
CD
|
E:GLU129
|
2.8
|
11.0
|
1.0
|
O
|
E:HOH472
|
2.9
|
11.5
|
1.0
|
CD
|
E:GLU357
|
3.0
|
8.5
|
1.0
|
O
|
E:HOH473
|
3.2
|
18.2
|
1.0
|
OE1
|
E:GLU357
|
3.3
|
8.5
|
1.0
|
CG
|
E:HIS269
|
3.3
|
10.4
|
1.0
|
OE1
|
E:GLU129
|
3.4
|
11.0
|
1.0
|
CG
|
E:GLU129
|
3.8
|
11.0
|
1.0
|
NE2
|
E:HIS271
|
3.9
|
14.3
|
1.0
|
CB
|
E:HIS269
|
3.9
|
10.4
|
1.0
|
NE2
|
E:HIS269
|
3.9
|
10.4
|
1.0
|
CD2
|
E:HIS269
|
4.2
|
10.4
|
1.0
|
CG
|
E:GLU357
|
4.2
|
8.5
|
1.0
|
CE1
|
E:HIS271
|
4.4
|
14.3
|
1.0
|
CB
|
E:GLU129
|
4.8
|
11.0
|
1.0
|
O
|
E:HOH471
|
4.8
|
21.1
|
1.0
|
CD2
|
E:HIS271
|
4.8
|
14.3
|
1.0
|
NH1
|
E:ARG359
|
4.9
|
12.3
|
1.0
|
|
Reference:
M.M.Yamashita,
R.J.Almassy,
C.A.Janson,
D.Cascio,
D.Eisenberg.
Refined Atomic Model of Glutamine Synthetase at 3.5 A Resolution. J.Biol.Chem. V. 264 17681 1989.
ISSN: ISSN 0021-9258
PubMed: 2572586
Page generated: Sat Oct 5 14:11:38 2024
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