Manganese in PDB 9e92: Acanthamoeba Polyphaga Mimivirus R699
Protein crystallography data
The structure of Acanthamoeba Polyphaga Mimivirus R699, PDB code: 9e92
was solved by
C.Buhlheller,
S.J.Richards,
J.S.Kim,
T.Chen,
J.Wu,
H.Guo,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
60.97 /
1.50
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
69.153,
124.998,
72.757,
90,
118.3,
90
|
R / Rfree (%)
|
16.6 /
18.9
|
Manganese Binding Sites:
The binding sites of Manganese atom in the Acanthamoeba Polyphaga Mimivirus R699
(pdb code 9e92). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the
Acanthamoeba Polyphaga Mimivirus R699, PDB code: 9e92:
Jump to Manganese binding site number:
1;
2;
Manganese binding site 1 out
of 2 in 9e92
Go back to
Manganese Binding Sites List in 9e92
Manganese binding site 1 out
of 2 in the Acanthamoeba Polyphaga Mimivirus R699
 Mono view
 Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Acanthamoeba Polyphaga Mimivirus R699 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn502
b:13.0
occ:1.00
|
HE2
|
A:HIS216
|
1.4
|
12.9
|
0.0
|
OD2
|
A:ASP83
|
2.1
|
14.5
|
1.0
|
O2B
|
A:UDP501
|
2.1
|
14.9
|
0.9
|
NE2
|
A:HIS216
|
2.2
|
12.9
|
1.0
|
O2A
|
A:UDP501
|
2.2
|
14.8
|
0.9
|
OD2
|
A:ASP86
|
2.3
|
12.3
|
1.0
|
OD1
|
A:ASP86
|
2.4
|
11.5
|
1.0
|
CG
|
A:ASP86
|
2.6
|
11.8
|
1.0
|
H5'1
|
A:UDP501
|
3.1
|
16.3
|
0.9
|
CG
|
A:ASP83
|
3.1
|
11.4
|
1.0
|
HB3
|
A:ASP83
|
3.2
|
12.5
|
1.0
|
CD2
|
A:HIS216
|
3.2
|
12.6
|
1.0
|
CE1
|
A:HIS216
|
3.2
|
14.1
|
1.0
|
PB
|
A:UDP501
|
3.3
|
17.4
|
0.9
|
HD2
|
A:HIS216
|
3.4
|
12.7
|
1.0
|
HE1
|
A:HIS216
|
3.4
|
13.6
|
1.0
|
PA
|
A:UDP501
|
3.4
|
19.3
|
0.9
|
O3A
|
A:UDP501
|
3.5
|
24.0
|
0.9
|
CB
|
A:ASP83
|
3.5
|
13.1
|
1.0
|
HO2
|
C:GLC2
|
3.6
|
14.1
|
0.9
|
HB2
|
A:ASP83
|
3.6
|
12.5
|
1.0
|
HA
|
A:ASN218
|
3.6
|
14.5
|
1.0
|
HO3'
|
A:UDP501
|
3.6
|
14.6
|
0.0
|
HO3
|
C:GLC2
|
3.9
|
13.1
|
0.9
|
O3'
|
A:UDP501
|
3.9
|
14.6
|
0.9
|
C5'
|
A:UDP501
|
4.0
|
16.1
|
0.9
|
HZ2
|
A:LYS222
|
4.0
|
15.7
|
1.0
|
O2
|
C:GLC2
|
4.1
|
14.1
|
0.9
|
H3
|
C:GLC2
|
4.1
|
13.7
|
0.9
|
CB
|
A:ASP86
|
4.1
|
12.4
|
1.0
|
O1B
|
A:UDP501
|
4.1
|
18.4
|
0.9
|
O5'
|
A:UDP501
|
4.3
|
17.2
|
0.9
|
HZ3
|
A:LYS222
|
4.3
|
15.7
|
1.0
|
OD1
|
A:ASP83
|
4.3
|
12.9
|
1.0
|
HB3
|
A:ASN218
|
4.4
|
13.8
|
1.0
|
ND1
|
A:HIS216
|
4.4
|
13.4
|
1.0
|
O3
|
C:GLC2
|
4.4
|
13.0
|
0.9
|
CG
|
A:HIS216
|
4.4
|
12.5
|
1.0
|
O3B
|
A:UDP501
|
4.5
|
28.5
|
0.9
|
HB3
|
A:ASP86
|
4.5
|
12.0
|
1.0
|
CA
|
A:ASN218
|
4.5
|
14.8
|
1.0
|
H
|
A:ASP86
|
4.5
|
12.1
|
1.0
|
HB2
|
A:ASP86
|
4.5
|
12.0
|
1.0
|
H4'
|
A:UDP501
|
4.6
|
15.8
|
0.9
|
HB2
|
A:ASN218
|
4.6
|
13.8
|
1.0
|
H
|
A:GLY219
|
4.6
|
16.6
|
1.0
|
O1A
|
A:UDP501
|
4.6
|
26.8
|
0.9
|
NZ
|
A:LYS222
|
4.6
|
15.0
|
1.0
|
HA3
|
A:GLY140
|
4.6
|
13.5
|
1.0
|
C4'
|
A:UDP501
|
4.6
|
15.8
|
0.9
|
C3
|
C:GLC2
|
4.7
|
13.4
|
0.9
|
H5'2
|
A:UDP501
|
4.7
|
16.3
|
0.9
|
C3'
|
A:UDP501
|
4.7
|
16.5
|
0.9
|
CB
|
A:ASN218
|
4.7
|
13.2
|
1.0
|
HB2
|
A:LEU87
|
4.8
|
10.9
|
1.0
|
HO2
|
C:BGC1
|
4.8
|
25.8
|
0.0
|
O
|
A:ASP86
|
5.0
|
11.5
|
1.0
|
|
Manganese binding site 2 out
of 2 in 9e92
Go back to
Manganese Binding Sites List in 9e92
Manganese binding site 2 out
of 2 in the Acanthamoeba Polyphaga Mimivirus R699
 Mono view
 Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Acanthamoeba Polyphaga Mimivirus R699 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn502
b:12.4
occ:1.00
|
HE2
|
B:HIS216
|
1.3
|
12.9
|
0.0
|
OD2
|
B:ASP83
|
2.1
|
13.9
|
1.0
|
NE2
|
B:HIS216
|
2.2
|
12.9
|
1.0
|
O2B
|
B:UDP501
|
2.2
|
8.9
|
0.5
|
OD2
|
B:ASP86
|
2.2
|
12.2
|
1.0
|
O2A
|
B:UDP501
|
2.2
|
11.9
|
0.5
|
OD1
|
B:ASP86
|
2.4
|
11.9
|
1.0
|
CG
|
B:ASP86
|
2.6
|
11.6
|
1.0
|
HO3'
|
B:UDP501
|
2.9
|
15.4
|
0.0
|
H5'1
|
B:UDP501
|
3.1
|
20.4
|
0.5
|
CG
|
B:ASP83
|
3.1
|
14.6
|
1.0
|
CE1
|
B:HIS216
|
3.2
|
13.1
|
1.0
|
HB3
|
B:ASP83
|
3.2
|
13.4
|
1.0
|
CD2
|
B:HIS216
|
3.2
|
11.1
|
1.0
|
HE1
|
B:HIS216
|
3.3
|
13.0
|
1.0
|
PB
|
B:UDP501
|
3.4
|
18.0
|
0.5
|
PA
|
B:UDP501
|
3.4
|
23.5
|
0.5
|
HD2
|
B:HIS216
|
3.4
|
11.7
|
1.0
|
HB2
|
B:ASP83
|
3.5
|
13.4
|
1.0
|
CB
|
B:ASP83
|
3.5
|
13.0
|
1.0
|
HA
|
B:ASN218
|
3.6
|
12.8
|
1.0
|
O3A
|
B:UDP501
|
3.6
|
18.8
|
0.5
|
C5'
|
B:UDP501
|
4.0
|
20.3
|
0.5
|
O1B
|
B:UDP501
|
4.1
|
16.0
|
0.5
|
CB
|
B:ASP86
|
4.2
|
11.7
|
1.0
|
O3'
|
B:UDP501
|
4.2
|
15.6
|
0.5
|
OD1
|
B:ASP83
|
4.3
|
16.2
|
1.0
|
ND1
|
B:HIS216
|
4.3
|
12.8
|
1.0
|
O5'
|
B:UDP501
|
4.4
|
21.6
|
0.5
|
HB3
|
B:ASN218
|
4.4
|
12.7
|
1.0
|
CG
|
B:HIS216
|
4.4
|
12.0
|
1.0
|
H
|
B:GLY219
|
4.4
|
14.6
|
1.0
|
CA
|
B:ASN218
|
4.5
|
13.1
|
1.0
|
HB3
|
B:ASP86
|
4.5
|
11.6
|
1.0
|
HB2
|
B:ASP86
|
4.5
|
11.6
|
1.0
|
H4'
|
B:UDP501
|
4.6
|
19.6
|
0.5
|
O1A
|
B:UDP501
|
4.6
|
22.5
|
0.5
|
C4'
|
B:UDP501
|
4.6
|
19.8
|
0.5
|
HB2
|
B:ASN218
|
4.6
|
12.7
|
1.0
|
H
|
B:ASP86
|
4.6
|
12.1
|
1.0
|
O3B
|
B:UDP501
|
4.6
|
19.1
|
0.5
|
H5'2
|
B:UDP501
|
4.7
|
20.5
|
0.5
|
HA3
|
B:GLY140
|
4.7
|
14.5
|
1.0
|
C3'
|
B:UDP501
|
4.7
|
18.3
|
0.5
|
O
|
B:HOH797
|
4.7
|
15.5
|
1.0
|
CB
|
B:ASN218
|
4.8
|
12.6
|
1.0
|
HB2
|
B:LEU87
|
4.9
|
12.0
|
1.0
|
H3'
|
B:UDP501
|
5.0
|
18.2
|
0.5
|
|
Reference:
S.J.Richards,
C.Buhlheller,
J.S.Kim,
T.Chen,
J.Wu,
H.Guo.
Acanthamoeba Polyphaga Mimivirus R699 To Be Published.
Page generated: Sun Aug 17 02:26:41 2025
|