Magnesium in PDB 3eoj: Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution
Protein crystallography data
The structure of Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution, PDB code: 3eoj
was solved by
D.E.Tronrud,
J.Wen,
L.Gay,
R.E.Blankenship,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
50.00 /
1.30
|
|
Space group
|
P 63
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
111.242,
111.242,
98.198,
90.00,
90.00,
120.00
|
|
R / Rfree (%)
|
13.5 /
16.1
|
Other elements in 3eoj:
The structure of Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution
(pdb code 3eoj). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 8 binding sites of Magnesium where determined in the
Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution, PDB code: 3eoj:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Magnesium binding site 1 out
of 8 in 3eoj
Go back to
Magnesium Binding Sites List in 3eoj
Magnesium binding site 1 out
of 8 in the Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg371
b:12.7
occ:1.00
|
MG
|
A:BCL371
|
0.0
|
12.7
|
1.0
|
|
ND
|
A:BCL371
|
2.0
|
12.1
|
1.0
|
|
NB
|
A:BCL371
|
2.0
|
12.0
|
1.0
|
|
NC
|
A:BCL371
|
2.1
|
12.6
|
1.0
|
|
NA
|
A:BCL371
|
2.2
|
11.9
|
1.0
|
|
NE2
|
A:HIS110
|
2.2
|
12.8
|
1.0
|
|
C4D
|
A:BCL371
|
3.0
|
12.1
|
1.0
|
|
C4B
|
A:BCL371
|
3.1
|
11.9
|
1.0
|
|
C1B
|
A:BCL371
|
3.1
|
12.4
|
1.0
|
|
C1C
|
A:BCL371
|
3.1
|
11.8
|
1.0
|
|
CE1
|
A:HIS110
|
3.1
|
14.1
|
1.0
|
|
C4A
|
A:BCL371
|
3.1
|
11.7
|
1.0
|
|
C1D
|
A:BCL371
|
3.1
|
11.5
|
1.0
|
|
C4C
|
A:BCL371
|
3.2
|
11.7
|
1.0
|
|
C1A
|
A:BCL371
|
3.2
|
12.2
|
1.0
|
|
CD2
|
A:HIS110
|
3.2
|
14.0
|
1.0
|
|
CHC
|
A:BCL371
|
3.4
|
12.1
|
1.0
|
|
CHB
|
A:BCL371
|
3.4
|
12.6
|
1.0
|
|
CHA
|
A:BCL371
|
3.5
|
12.3
|
1.0
|
|
CHD
|
A:BCL371
|
3.5
|
12.1
|
1.0
|
|
C2
|
A:BCL371
|
3.8
|
13.6
|
1.0
|
|
C3
|
A:BCL371
|
3.8
|
12.7
|
1.0
|
|
C1
|
A:BCL371
|
4.2
|
14.1
|
1.0
|
|
C3D
|
A:BCL371
|
4.2
|
11.3
|
1.0
|
|
ND1
|
A:HIS110
|
4.2
|
14.6
|
1.0
|
|
C5
|
A:BCL371
|
4.2
|
12.8
|
1.0
|
|
C2B
|
A:BCL371
|
4.3
|
12.6
|
1.0
|
|
C4
|
A:BCL371
|
4.3
|
13.3
|
1.0
|
|
C3B
|
A:BCL371
|
4.3
|
11.9
|
1.0
|
|
C2D
|
A:BCL371
|
4.3
|
11.1
|
1.0
|
|
CG
|
A:HIS110
|
4.4
|
14.2
|
1.0
|
|
C2C
|
A:BCL371
|
4.4
|
10.8
|
1.0
|
|
C3A
|
A:BCL371
|
4.5
|
12.4
|
1.0
|
|
C3C
|
A:BCL371
|
4.5
|
11.8
|
1.0
|
|
C2A
|
A:BCL371
|
4.5
|
13.0
|
1.0
|
|
O2A
|
A:BCL371
|
4.6
|
13.9
|
1.0
|
|
CD2
|
A:LEU103
|
4.6
|
17.2
|
1.0
|
|
C6
|
A:BCL371
|
4.7
|
13.4
|
1.0
|
|
CBD
|
A:BCL371
|
5.0
|
12.3
|
1.0
|
|
Magnesium binding site 2 out
of 8 in 3eoj
Go back to
Magnesium Binding Sites List in 3eoj
Magnesium binding site 2 out
of 8 in the Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg372
b:10.5
occ:1.00
|
MG
|
A:BCL372
|
0.0
|
10.5
|
1.0
|
|
ND
|
A:BCL372
|
2.0
|
10.2
|
1.0
|
|
NB
|
A:BCL372
|
2.0
|
10.7
|
1.0
|
|
O
|
A:HOH1047
|
2.0
|
11.5
|
1.0
|
|
NC
|
A:BCL372
|
2.1
|
9.9
|
1.0
|
|
NA
|
A:BCL372
|
2.1
|
10.5
|
1.0
|
|
C4D
|
A:BCL372
|
3.0
|
10.0
|
1.0
|
|
C1B
|
A:BCL372
|
3.1
|
10.7
|
1.0
|
|
C4B
|
A:BCL372
|
3.1
|
10.8
|
1.0
|
|
C1C
|
A:BCL372
|
3.1
|
10.3
|
1.0
|
|
C4A
|
A:BCL372
|
3.1
|
10.4
|
1.0
|
|
C1D
|
A:BCL372
|
3.1
|
10.3
|
1.0
|
|
C4C
|
A:BCL372
|
3.1
|
9.9
|
1.0
|
|
C1A
|
A:BCL372
|
3.2
|
10.0
|
1.0
|
|
CHC
|
A:BCL372
|
3.4
|
10.6
|
1.0
|
|
CHB
|
A:BCL372
|
3.4
|
10.3
|
1.0
|
|
CHA
|
A:BCL372
|
3.4
|
9.7
|
1.0
|
|
CHD
|
A:BCL372
|
3.5
|
10.5
|
1.0
|
|
O
|
A:HOH1105
|
3.9
|
13.7
|
0.8
|
|
C12
|
A:BCL377
|
3.9
|
13.7
|
1.0
|
|
O
|
A:HOH1118
|
4.1
|
12.8
|
1.0
|
|
C3D
|
A:BCL372
|
4.2
|
9.4
|
1.0
|
|
C2D
|
A:BCL372
|
4.3
|
9.9
|
1.0
|
|
C3B
|
A:BCL372
|
4.3
|
11.7
|
1.0
|
|
C2B
|
A:BCL372
|
4.3
|
11.0
|
1.0
|
|
CG2
|
A:VAL74
|
4.4
|
13.1
|
1.0
|
|
C2C
|
A:BCL372
|
4.4
|
10.1
|
1.0
|
|
C3A
|
A:BCL372
|
4.5
|
10.9
|
1.0
|
|
ND2
|
A:ASN79
|
4.5
|
14.3
|
1.0
|
|
C3C
|
A:BCL372
|
4.5
|
10.2
|
1.0
|
|
O
|
A:HOH1105
|
4.5
|
13.0
|
0.2
|
|
C2A
|
A:BCL372
|
4.5
|
10.2
|
1.0
|
|
C10
|
A:BCL377
|
4.5
|
12.1
|
1.0
|
|
C11
|
A:BCL377
|
4.6
|
12.1
|
1.0
|
|
C13
|
A:BCL377
|
4.9
|
14.8
|
1.0
|
|
CG1
|
A:VAL74
|
4.9
|
12.4
|
1.0
|
|
CB
|
A:VAL74
|
4.9
|
10.8
|
1.0
|
|
CBD
|
A:BCL372
|
4.9
|
10.0
|
1.0
|
|
C14
|
A:BCL377
|
4.9
|
14.5
|
1.0
|
|
C15
|
A:BCL377
|
5.0
|
22.5
|
0.7
|
|
Magnesium binding site 3 out
of 8 in 3eoj
Go back to
Magnesium Binding Sites List in 3eoj
Magnesium binding site 3 out
of 8 in the Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg373
b:9.2
occ:1.00
|
MG
|
A:BCL373
|
0.0
|
9.2
|
1.0
|
|
ND
|
A:BCL373
|
2.0
|
8.6
|
1.0
|
|
NB
|
A:BCL373
|
2.1
|
9.0
|
1.0
|
|
NE2
|
A:HIS298
|
2.1
|
8.6
|
1.0
|
|
NC
|
A:BCL373
|
2.1
|
9.0
|
1.0
|
|
NA
|
A:BCL373
|
2.2
|
8.9
|
1.0
|
|
C4D
|
A:BCL373
|
3.0
|
8.8
|
1.0
|
|
C1C
|
A:BCL373
|
3.1
|
8.8
|
1.0
|
|
CE1
|
A:HIS298
|
3.1
|
8.7
|
1.0
|
|
C1B
|
A:BCL373
|
3.1
|
9.1
|
1.0
|
|
C4B
|
A:BCL373
|
3.1
|
9.0
|
1.0
|
|
C4A
|
A:BCL373
|
3.1
|
9.0
|
1.0
|
|
CD2
|
A:HIS298
|
3.1
|
8.8
|
1.0
|
|
C4C
|
A:BCL373
|
3.2
|
9.3
|
1.0
|
|
C1D
|
A:BCL373
|
3.2
|
8.4
|
1.0
|
|
C1A
|
A:BCL373
|
3.2
|
8.7
|
1.0
|
|
CHC
|
A:BCL373
|
3.4
|
9.0
|
1.0
|
|
CHB
|
A:BCL373
|
3.4
|
9.1
|
1.0
|
|
CHA
|
A:BCL373
|
3.5
|
8.9
|
1.0
|
|
CHD
|
A:BCL373
|
3.5
|
9.0
|
1.0
|
|
C3D
|
A:BCL373
|
4.2
|
8.9
|
1.0
|
|
ND1
|
A:HIS298
|
4.2
|
8.5
|
1.0
|
|
CG
|
A:HIS298
|
4.3
|
8.1
|
1.0
|
|
C3B
|
A:BCL373
|
4.3
|
9.2
|
1.0
|
|
C2B
|
A:BCL373
|
4.3
|
9.3
|
1.0
|
|
C2D
|
A:BCL373
|
4.4
|
8.5
|
1.0
|
|
C2C
|
A:BCL373
|
4.4
|
9.1
|
1.0
|
|
C3C
|
A:BCL373
|
4.5
|
10.0
|
1.0
|
|
C3A
|
A:BCL373
|
4.5
|
10.2
|
1.0
|
|
C2A
|
A:BCL373
|
4.5
|
9.4
|
1.0
|
|
CBC
|
A:BCL374
|
4.5
|
11.3
|
1.0
|
|
CD1
|
A:ILE265
|
4.8
|
11.6
|
1.0
|
|
CG2
|
A:VAL301
|
4.9
|
11.9
|
1.0
|
|
CBD
|
A:BCL373
|
4.9
|
8.5
|
1.0
|
|
Magnesium binding site 4 out
of 8 in 3eoj
Go back to
Magnesium Binding Sites List in 3eoj
Magnesium binding site 4 out
of 8 in the Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg374
b:10.2
occ:1.00
|
MG
|
A:BCL374
|
0.0
|
10.2
|
1.0
|
|
ND
|
A:BCL374
|
2.0
|
9.7
|
1.0
|
|
NB
|
A:BCL374
|
2.1
|
9.6
|
1.0
|
|
NE2
|
A:HIS290
|
2.1
|
9.7
|
1.0
|
|
NC
|
A:BCL374
|
2.1
|
9.6
|
1.0
|
|
NA
|
A:BCL374
|
2.2
|
10.7
|
1.0
|
|
C4D
|
A:BCL374
|
3.0
|
9.7
|
1.0
|
|
CE1
|
A:HIS290
|
3.0
|
9.9
|
1.0
|
|
C1B
|
A:BCL374
|
3.1
|
9.4
|
1.0
|
|
C4A
|
A:BCL374
|
3.1
|
11.0
|
1.0
|
|
C1C
|
A:BCL374
|
3.1
|
9.2
|
1.0
|
|
C4B
|
A:BCL374
|
3.1
|
9.6
|
1.0
|
|
C1D
|
A:BCL374
|
3.1
|
9.7
|
1.0
|
|
C4C
|
A:BCL374
|
3.1
|
9.3
|
1.0
|
|
CD2
|
A:HIS290
|
3.1
|
10.4
|
1.0
|
|
C1A
|
A:BCL374
|
3.2
|
10.1
|
1.0
|
|
CHB
|
A:BCL374
|
3.4
|
10.4
|
1.0
|
|
CHC
|
A:BCL374
|
3.4
|
9.6
|
1.0
|
|
CHA
|
A:BCL374
|
3.5
|
9.9
|
1.0
|
|
CHD
|
A:BCL374
|
3.5
|
9.2
|
1.0
|
|
ND1
|
A:HIS290
|
4.2
|
9.7
|
1.0
|
|
C4
|
A:BCL374
|
4.2
|
11.6
|
1.0
|
|
C3D
|
A:BCL374
|
4.2
|
10.0
|
1.0
|
|
CG
|
A:HIS290
|
4.2
|
10.2
|
1.0
|
|
C2B
|
A:BCL374
|
4.3
|
10.0
|
1.0
|
|
C3B
|
A:BCL374
|
4.3
|
9.6
|
1.0
|
|
C2D
|
A:BCL374
|
4.3
|
9.5
|
1.0
|
|
C3A
|
A:BCL374
|
4.4
|
11.1
|
1.0
|
|
C3C
|
A:BCL374
|
4.4
|
8.8
|
1.0
|
|
C2C
|
A:BCL374
|
4.4
|
9.2
|
1.0
|
|
C2A
|
A:BCL374
|
4.5
|
11.0
|
1.0
|
|
O2A
|
A:BCL374
|
4.6
|
11.7
|
1.0
|
|
C4
|
A:BCL375
|
4.8
|
16.6
|
1.0
|
|
C3
|
A:BCL374
|
4.8
|
10.9
|
1.0
|
|
CBD
|
A:BCL374
|
4.9
|
10.7
|
1.0
|
|
CMA
|
A:BCL374
|
5.0
|
12.4
|
1.0
|
|
Magnesium binding site 5 out
of 8 in 3eoj
Go back to
Magnesium Binding Sites List in 3eoj
Magnesium binding site 5 out
of 8 in the Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg375
b:10.6
occ:1.00
|
MG
|
A:BCL375
|
0.0
|
10.6
|
1.0
|
|
ND
|
A:BCL375
|
2.0
|
9.5
|
1.0
|
|
NB
|
A:BCL375
|
2.0
|
10.6
|
1.0
|
|
O
|
A:LEU242
|
2.0
|
10.3
|
1.0
|
|
NC
|
A:BCL375
|
2.1
|
10.1
|
1.0
|
|
NA
|
A:BCL375
|
2.2
|
10.2
|
1.0
|
|
C4D
|
A:BCL375
|
3.0
|
9.5
|
1.0
|
|
C4B
|
A:BCL375
|
3.0
|
10.8
|
1.0
|
|
C1B
|
A:BCL375
|
3.1
|
11.2
|
1.0
|
|
C1C
|
A:BCL375
|
3.1
|
10.7
|
1.0
|
|
C4A
|
A:BCL375
|
3.1
|
10.7
|
1.0
|
|
C1D
|
A:BCL375
|
3.1
|
9.8
|
1.0
|
|
C4C
|
A:BCL375
|
3.2
|
9.9
|
1.0
|
|
C1A
|
A:BCL375
|
3.2
|
9.8
|
1.0
|
|
C
|
A:LEU242
|
3.2
|
10.4
|
1.0
|
|
CHC
|
A:BCL375
|
3.4
|
11.1
|
1.0
|
|
CHB
|
A:BCL375
|
3.4
|
11.0
|
1.0
|
|
CHA
|
A:BCL375
|
3.5
|
9.8
|
1.0
|
|
CHD
|
A:BCL375
|
3.5
|
9.6
|
1.0
|
|
CA
|
A:LEU242
|
3.9
|
10.2
|
1.0
|
|
CB
|
A:LEU242
|
3.9
|
10.6
|
1.0
|
|
C12
|
A:BCL376
|
4.2
|
23.9
|
1.0
|
|
C3D
|
A:BCL375
|
4.2
|
9.6
|
1.0
|
|
C3B
|
A:BCL375
|
4.3
|
11.4
|
1.0
|
|
N
|
A:PHE243
|
4.3
|
10.4
|
1.0
|
|
C2B
|
A:BCL375
|
4.3
|
11.6
|
1.0
|
|
C2D
|
A:BCL375
|
4.3
|
9.9
|
1.0
|
|
CD1
|
A:LEU242
|
4.3
|
11.4
|
1.0
|
|
C3A
|
A:BCL375
|
4.4
|
10.8
|
1.0
|
|
C2C
|
A:BCL375
|
4.4
|
10.8
|
1.0
|
|
C15
|
A:BCL376
|
4.4
|
20.7
|
1.0
|
|
C3C
|
A:BCL375
|
4.5
|
10.6
|
1.0
|
|
C2A
|
A:BCL375
|
4.5
|
10.1
|
1.0
|
|
CA
|
A:PHE243
|
4.6
|
10.9
|
1.0
|
|
CD
|
A:PRO244
|
4.7
|
12.3
|
1.0
|
|
CG
|
A:LEU242
|
4.8
|
10.4
|
1.0
|
|
CBD
|
A:BCL375
|
4.9
|
10.1
|
1.0
|
|
C13
|
A:BCL376
|
5.0
|
17.2
|
1.0
|
|
CMA
|
A:BCL375
|
5.0
|
12.2
|
1.0
|
|
C16
|
A:BCL376
|
5.0
|
17.5
|
1.0
|
|
Magnesium binding site 6 out
of 8 in 3eoj
Go back to
Magnesium Binding Sites List in 3eoj
Magnesium binding site 6 out
of 8 in the Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg376
b:10.3
occ:1.00
|
MG
|
A:BCL376
|
0.0
|
10.3
|
1.0
|
|
ND
|
A:BCL376
|
2.0
|
9.3
|
1.0
|
|
NB
|
A:BCL376
|
2.1
|
9.8
|
1.0
|
|
NC
|
A:BCL376
|
2.1
|
9.2
|
0.4
|
|
NC
|
A:BCL376
|
2.1
|
9.1
|
0.6
|
|
NE2
|
A:HIS145
|
2.2
|
10.2
|
1.0
|
|
NA
|
A:BCL376
|
2.2
|
10.2
|
1.0
|
|
C4D
|
A:BCL376
|
3.0
|
9.8
|
0.6
|
|
C4D
|
A:BCL376
|
3.0
|
9.9
|
0.4
|
|
C1C
|
A:BCL376
|
3.1
|
9.0
|
0.6
|
|
C4C
|
A:BCL376
|
3.1
|
9.1
|
0.4
|
|
C1C
|
A:BCL376
|
3.1
|
9.0
|
0.4
|
|
C4B
|
A:BCL376
|
3.1
|
10.2
|
1.0
|
|
CD2
|
A:HIS145
|
3.1
|
9.7
|
1.0
|
|
C1B
|
A:BCL376
|
3.1
|
10.1
|
1.0
|
|
C1D
|
A:BCL376
|
3.1
|
9.7
|
1.0
|
|
C4C
|
A:BCL376
|
3.1
|
9.3
|
0.6
|
|
C4A
|
A:BCL376
|
3.2
|
10.8
|
1.0
|
|
CE1
|
A:HIS145
|
3.2
|
10.5
|
1.0
|
|
C1A
|
A:BCL376
|
3.2
|
10.9
|
1.0
|
|
CHC
|
A:BCL376
|
3.4
|
9.6
|
1.0
|
|
CHB
|
A:BCL376
|
3.5
|
11.2
|
1.0
|
|
CHD
|
A:BCL376
|
3.5
|
9.1
|
1.0
|
|
CHA
|
A:BCL376
|
3.5
|
10.5
|
0.6
|
|
CHA
|
A:BCL376
|
3.5
|
10.5
|
0.4
|
|
C19
|
A:BCL373
|
3.8
|
17.2
|
0.4
|
|
C20
|
A:BCL373
|
4.1
|
19.2
|
0.6
|
|
C3D
|
A:BCL376
|
4.2
|
9.5
|
0.6
|
|
C3D
|
A:BCL376
|
4.2
|
9.9
|
0.4
|
|
CG
|
A:HIS145
|
4.3
|
10.0
|
1.0
|
|
C2D
|
A:BCL376
|
4.3
|
9.7
|
1.0
|
|
C18
|
A:BCL373
|
4.3
|
17.5
|
0.6
|
|
ND1
|
A:HIS145
|
4.3
|
10.5
|
1.0
|
|
C2B
|
A:BCL376
|
4.3
|
10.5
|
1.0
|
|
C3B
|
A:BCL376
|
4.3
|
9.7
|
1.0
|
|
C2C
|
A:BCL376
|
4.4
|
9.2
|
0.4
|
|
C2C
|
A:BCL376
|
4.4
|
9.2
|
0.6
|
|
C3C
|
A:BCL376
|
4.4
|
9.9
|
0.4
|
|
C3C
|
A:BCL376
|
4.5
|
9.9
|
0.6
|
|
C3A
|
A:BCL376
|
4.5
|
11.6
|
1.0
|
|
C2A
|
A:BCL376
|
4.5
|
11.2
|
1.0
|
|
C19
|
A:BCL373
|
4.6
|
16.9
|
0.6
|
|
C20
|
A:BCL373
|
4.8
|
16.9
|
0.4
|
|
C18
|
A:BCL373
|
4.8
|
16.1
|
0.4
|
|
CBD
|
A:BCL376
|
4.9
|
10.7
|
0.4
|
|
CZ
|
A:PHE225
|
5.0
|
12.2
|
1.0
|
|
CBD
|
A:BCL376
|
5.0
|
10.3
|
0.6
|
|
CG2
|
A:VAL118
|
5.0
|
12.4
|
1.0
|
|
Magnesium binding site 7 out
of 8 in 3eoj
Go back to
Magnesium Binding Sites List in 3eoj
Magnesium binding site 7 out
of 8 in the Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 7 of Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg377
b:8.8
occ:1.00
|
MG
|
A:BCL377
|
0.0
|
8.8
|
1.0
|
|
ND
|
A:BCL377
|
2.0
|
8.7
|
1.0
|
|
NB
|
A:BCL377
|
2.1
|
8.3
|
1.0
|
|
NC
|
A:BCL377
|
2.1
|
8.7
|
1.0
|
|
ND1
|
A:HIS297
|
2.1
|
8.2
|
1.0
|
|
NA
|
A:BCL377
|
2.2
|
8.6
|
1.0
|
|
C4D
|
A:BCL377
|
3.0
|
8.2
|
1.0
|
|
C1B
|
A:BCL377
|
3.0
|
8.7
|
1.0
|
|
C4B
|
A:BCL377
|
3.1
|
8.5
|
1.0
|
|
CE1
|
A:HIS297
|
3.1
|
8.7
|
1.0
|
|
C1C
|
A:BCL377
|
3.1
|
8.9
|
0.5
|
|
C1C
|
A:BCL377
|
3.1
|
9.1
|
0.5
|
|
C4A
|
A:BCL377
|
3.1
|
7.9
|
1.0
|
|
C1D
|
A:BCL377
|
3.1
|
8.8
|
1.0
|
|
C4C
|
A:BCL377
|
3.2
|
9.0
|
0.5
|
|
C4C
|
A:BCL377
|
3.2
|
9.0
|
0.5
|
|
C1A
|
A:BCL377
|
3.2
|
8.0
|
1.0
|
|
CG
|
A:HIS297
|
3.2
|
7.8
|
1.0
|
|
CHB
|
A:BCL377
|
3.4
|
8.7
|
1.0
|
|
CHC
|
A:BCL377
|
3.4
|
9.1
|
1.0
|
|
CHA
|
A:BCL377
|
3.5
|
8.6
|
1.0
|
|
CHD
|
A:BCL377
|
3.5
|
9.1
|
1.0
|
|
CB
|
A:HIS297
|
3.6
|
8.3
|
1.0
|
|
C4
|
A:BCL373
|
3.6
|
14.0
|
1.0
|
|
C3D
|
A:BCL377
|
4.2
|
8.4
|
1.0
|
|
C2B
|
A:BCL377
|
4.2
|
9.6
|
1.0
|
|
NE2
|
A:HIS297
|
4.2
|
8.7
|
1.0
|
|
C3B
|
A:BCL377
|
4.2
|
9.2
|
0.6
|
|
C3B
|
A:BCL377
|
4.2
|
9.3
|
0.4
|
|
CD2
|
A:HIS297
|
4.3
|
8.1
|
1.0
|
|
C2D
|
A:BCL377
|
4.3
|
8.5
|
1.0
|
|
C3
|
A:BCL373
|
4.4
|
12.1
|
1.0
|
|
C2C
|
A:BCL377
|
4.5
|
9.8
|
0.5
|
|
C2C
|
A:BCL377
|
4.5
|
9.1
|
0.5
|
|
CG2
|
A:ILE293
|
4.5
|
9.5
|
1.0
|
|
C3A
|
A:BCL377
|
4.5
|
8.7
|
1.0
|
|
C3C
|
A:BCL377
|
4.5
|
9.5
|
0.5
|
|
C3C
|
A:BCL377
|
4.5
|
9.5
|
0.5
|
|
C2A
|
A:BCL377
|
4.5
|
8.8
|
1.0
|
|
CBD
|
A:BCL377
|
5.0
|
8.8
|
1.0
|
|
Magnesium binding site 8 out
of 8 in 3eoj
Go back to
Magnesium Binding Sites List in 3eoj
Magnesium binding site 8 out
of 8 in the Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 8 of Fmo Protein From Prosthecochloris Aestuarii 2K at 1.3A Resolution within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg378
b:13.8
occ:0.34
|
MG
|
A:BCL378
|
0.0
|
13.8
|
0.3
|
|
CD1
|
A:TYR124
|
1.8
|
14.1
|
0.7
|
|
CE1
|
A:TYR124
|
1.8
|
13.1
|
0.7
|
|
ND
|
A:BCL378
|
2.0
|
16.2
|
0.3
|
|
NB
|
A:BCL378
|
2.0
|
18.0
|
0.3
|
|
O
|
A:TYR123
|
2.1
|
14.4
|
0.3
|
|
NC
|
A:BCL378
|
2.1
|
14.6
|
0.3
|
|
NA
|
A:BCL378
|
2.1
|
19.3
|
0.3
|
|
O
|
A:HOH1304
|
2.2
|
21.8
|
0.7
|
|
CZ
|
A:TYR124
|
2.6
|
12.9
|
0.7
|
|
CG
|
A:TYR124
|
2.6
|
12.7
|
0.7
|
|
O
|
A:HOH2105
|
2.7
|
27.7
|
0.7
|
|
O
|
A:HOH1309
|
2.9
|
23.5
|
0.7
|
|
C4D
|
A:BCL378
|
3.0
|
18.7
|
0.3
|
|
C4B
|
A:BCL378
|
3.1
|
14.8
|
0.3
|
|
C1B
|
A:BCL378
|
3.1
|
19.3
|
0.3
|
|
C1C
|
A:BCL378
|
3.1
|
14.6
|
0.3
|
|
C4A
|
A:BCL378
|
3.1
|
19.2
|
0.3
|
|
C1D
|
A:BCL378
|
3.1
|
15.2
|
0.3
|
|
C4C
|
A:BCL378
|
3.2
|
14.8
|
0.3
|
|
C1A
|
A:BCL378
|
3.2
|
21.8
|
0.3
|
|
CD2
|
A:TYR124
|
3.2
|
12.7
|
0.7
|
|
CE2
|
A:TYR124
|
3.2
|
11.7
|
0.7
|
|
C
|
A:TYR123
|
3.3
|
12.9
|
0.3
|
|
N
|
A:TYR124
|
3.3
|
12.2
|
0.7
|
|
CHC
|
A:BCL378
|
3.4
|
14.1
|
0.3
|
|
CHB
|
A:BCL378
|
3.4
|
20.4
|
0.3
|
|
CHA
|
A:BCL378
|
3.5
|
20.4
|
0.3
|
|
CHD
|
A:BCL378
|
3.5
|
14.3
|
0.3
|
|
OH
|
A:TYR124
|
3.5
|
14.2
|
0.7
|
|
CA
|
A:TYR124
|
3.6
|
12.6
|
0.7
|
|
CB
|
A:TYR124
|
3.7
|
12.3
|
0.7
|
|
O
|
A:HOH2231
|
4.2
|
22.9
|
0.7
|
|
CA
|
A:TYR123
|
4.2
|
13.0
|
0.3
|
|
C3D
|
A:BCL378
|
4.2
|
18.6
|
0.3
|
|
C2B
|
A:BCL378
|
4.3
|
18.0
|
0.3
|
|
N
|
A:TYR124
|
4.3
|
12.6
|
0.3
|
|
C3B
|
A:BCL378
|
4.3
|
15.3
|
0.3
|
|
C
|
A:TYR123
|
4.3
|
11.3
|
0.7
|
|
C2D
|
A:BCL378
|
4.3
|
15.8
|
0.3
|
|
CA
|
A:TYR124
|
4.3
|
13.3
|
0.3
|
|
O
|
A:HOH1310
|
4.4
|
10.4
|
0.7
|
|
C3A
|
A:BCL378
|
4.4
|
20.5
|
0.3
|
|
C2C
|
A:BCL378
|
4.4
|
15.3
|
0.3
|
|
C3C
|
A:BCL378
|
4.5
|
16.2
|
0.3
|
|
C2A
|
A:BCL378
|
4.5
|
21.9
|
0.3
|
|
CA
|
A:TYR123
|
4.5
|
12.1
|
0.7
|
|
CB
|
A:TYR123
|
4.7
|
12.4
|
0.3
|
|
CB
|
A:TYR124
|
4.8
|
12.9
|
0.3
|
|
CBD
|
A:BCL378
|
4.9
|
21.0
|
0.3
|
|
Reference:
D.E.Tronrud,
J.Wen,
L.Gay,
R.E.Blankenship.
The Structural Basis For the Difference in Absorbance Spectra For the Fmo Antenna Protein From Various Green Sulfur Bacteria. Photosynth.Res. V. 100 79 2009.
ISSN: ISSN 0166-8595
PubMed: 19437128
DOI: 10.1007/S11120-009-9430-6
Page generated: Sun Aug 10 20:33:02 2025
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