Magnesium in PDB 2m2u: Binary Complex of African Swine Fever Virus Pol X with Mgdgtp
Enzymatic activity of Binary Complex of African Swine Fever Virus Pol X with Mgdgtp
All present enzymatic activity of Binary Complex of African Swine Fever Virus Pol X with Mgdgtp:
2.7.7.7;
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Binary Complex of African Swine Fever Virus Pol X with Mgdgtp
(pdb code 2m2u). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the
Binary Complex of African Swine Fever Virus Pol X with Mgdgtp, PDB code: 2m2u:
Jump to Magnesium binding site number:
1;
2;
Magnesium binding site 1 out
of 2 in 2m2u
Go back to
Magnesium Binding Sites List in 2m2u
Magnesium binding site 1 out
of 2 in the Binary Complex of African Swine Fever Virus Pol X with Mgdgtp
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Binary Complex of African Swine Fever Virus Pol X with Mgdgtp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg202
b:0.5
occ:1.00
|
OD2
|
A:ASP51
|
1.5
|
0.4
|
1.0
|
OD2
|
A:ASP100
|
1.6
|
0.4
|
1.0
|
OD1
|
A:ASP49
|
1.6
|
1.0
|
1.0
|
CG
|
A:ASP51
|
2.5
|
0.3
|
1.0
|
HB2
|
A:ASP100
|
2.5
|
0.5
|
1.0
|
CG
|
A:ASP100
|
2.6
|
0.4
|
1.0
|
CG
|
A:ASP49
|
2.6
|
0.5
|
1.0
|
O1A
|
A:DGT201
|
2.8
|
1.3
|
1.0
|
OD1
|
A:ASP51
|
2.9
|
0.4
|
1.0
|
OD2
|
A:ASP49
|
3.0
|
1.1
|
1.0
|
CB
|
A:ASP100
|
3.0
|
0.3
|
1.0
|
HB3
|
A:ASP100
|
3.5
|
0.6
|
1.0
|
O3A
|
A:DGT201
|
3.6
|
0.7
|
1.0
|
OD1
|
A:ASP100
|
3.6
|
0.7
|
1.0
|
MG
|
A:MG203
|
3.7
|
0.8
|
1.0
|
PA
|
A:DGT201
|
3.7
|
0.9
|
1.0
|
CB
|
A:ASP51
|
3.8
|
0.3
|
1.0
|
CB
|
A:ASP49
|
3.9
|
0.4
|
1.0
|
HB3
|
A:ASP51
|
4.0
|
0.3
|
1.0
|
HB2
|
A:ASP49
|
4.0
|
0.5
|
1.0
|
H
|
A:ASP100
|
4.0
|
0.3
|
1.0
|
O3G
|
A:DGT201
|
4.1
|
0.9
|
1.0
|
HA
|
A:ASP51
|
4.2
|
0.3
|
1.0
|
O2A
|
A:DGT201
|
4.3
|
1.0
|
1.0
|
CA
|
A:ASP100
|
4.3
|
0.3
|
1.0
|
O
|
A:ASP49
|
4.4
|
0.4
|
1.0
|
N
|
A:ASP100
|
4.4
|
0.2
|
1.0
|
CA
|
A:ASP51
|
4.5
|
0.2
|
1.0
|
C
|
A:ASP49
|
4.6
|
0.3
|
1.0
|
HB2
|
A:ASP51
|
4.6
|
0.3
|
1.0
|
O
|
A:VAL50
|
4.6
|
0.3
|
1.0
|
HB3
|
A:ASP49
|
4.6
|
0.6
|
1.0
|
N
|
A:ASP51
|
4.7
|
0.2
|
1.0
|
HN2
|
A:DGT201
|
4.7
|
1.4
|
1.0
|
N2
|
A:DGT201
|
4.7
|
1.0
|
1.0
|
C
|
A:VAL50
|
4.7
|
0.2
|
1.0
|
HE1
|
A:PHE102
|
4.8
|
2.2
|
1.0
|
HN2A
|
A:DGT201
|
4.8
|
1.4
|
1.0
|
CA
|
A:ASP49
|
4.9
|
0.4
|
1.0
|
HE2
|
A:PHE116
|
4.9
|
2.2
|
1.0
|
HA
|
A:ASP100
|
4.9
|
0.3
|
1.0
|
H
|
A:ASP49
|
5.0
|
0.6
|
1.0
|
|
Magnesium binding site 2 out
of 2 in 2m2u
Go back to
Magnesium Binding Sites List in 2m2u
Magnesium binding site 2 out
of 2 in the Binary Complex of African Swine Fever Virus Pol X with Mgdgtp
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Binary Complex of African Swine Fever Virus Pol X with Mgdgtp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg203
b:0.8
occ:1.00
|
O3G
|
A:DGT201
|
1.3
|
0.9
|
1.0
|
O
|
A:ASP49
|
1.6
|
0.4
|
1.0
|
O2B
|
A:DGT201
|
2.1
|
0.7
|
1.0
|
H
|
A:ASP49
|
2.4
|
0.6
|
1.0
|
OD1
|
A:ASP51
|
2.5
|
0.4
|
1.0
|
C
|
A:ASP49
|
2.6
|
0.3
|
1.0
|
PG
|
A:DGT201
|
2.7
|
0.8
|
1.0
|
O3A
|
A:DGT201
|
2.8
|
0.7
|
1.0
|
OD1
|
A:ASP49
|
2.8
|
1.0
|
1.0
|
PB
|
A:DGT201
|
2.8
|
0.6
|
1.0
|
CG
|
A:ASP49
|
2.9
|
0.5
|
1.0
|
HD13
|
A:LEU47
|
2.9
|
1.7
|
1.0
|
N
|
A:ASP49
|
3.0
|
0.5
|
1.0
|
O2G
|
A:DGT201
|
3.1
|
1.0
|
1.0
|
CA
|
A:ASP49
|
3.2
|
0.4
|
1.0
|
O3B
|
A:DGT201
|
3.2
|
0.7
|
1.0
|
OD2
|
A:ASP49
|
3.3
|
1.1
|
1.0
|
CB
|
A:ASP49
|
3.6
|
0.4
|
1.0
|
CG
|
A:ASP51
|
3.6
|
0.3
|
1.0
|
MG
|
A:MG202
|
3.7
|
0.5
|
1.0
|
N
|
A:VAL50
|
3.8
|
0.3
|
1.0
|
O1G
|
A:DGT201
|
3.8
|
1.1
|
1.0
|
HB2
|
A:ASN48
|
3.8
|
1.2
|
1.0
|
HA
|
A:VAL50
|
3.8
|
0.3
|
1.0
|
CD1
|
A:LEU47
|
4.0
|
1.1
|
1.0
|
OD2
|
A:ASP51
|
4.0
|
0.4
|
1.0
|
HB2
|
A:LEU47
|
4.1
|
1.5
|
1.0
|
PA
|
A:DGT201
|
4.2
|
0.9
|
1.0
|
C
|
A:ASN48
|
4.2
|
0.5
|
1.0
|
H
|
A:ASN48
|
4.2
|
0.7
|
1.0
|
HA
|
A:ASP49
|
4.2
|
0.4
|
1.0
|
HD11
|
A:LEU47
|
4.2
|
1.7
|
1.0
|
HB2
|
A:ASP49
|
4.2
|
0.5
|
1.0
|
CA
|
A:VAL50
|
4.2
|
0.3
|
1.0
|
O1B
|
A:DGT201
|
4.3
|
0.8
|
1.0
|
H
|
A:ASP51
|
4.3
|
0.2
|
1.0
|
HB3
|
A:ASP49
|
4.4
|
0.6
|
1.0
|
HD12
|
A:LEU47
|
4.5
|
1.6
|
1.0
|
O2A
|
A:DGT201
|
4.5
|
1.0
|
1.0
|
O1A
|
A:DGT201
|
4.5
|
1.3
|
1.0
|
HD22
|
A:LEU47
|
4.5
|
1.6
|
1.0
|
H
|
A:VAL50
|
4.5
|
0.3
|
1.0
|
C
|
A:VAL50
|
4.5
|
0.2
|
1.0
|
N
|
A:ASP51
|
4.6
|
0.2
|
1.0
|
N
|
A:ASN48
|
4.6
|
0.6
|
1.0
|
HA3
|
A:GLY38
|
4.6
|
0.3
|
1.0
|
CB
|
A:ASN48
|
4.7
|
0.8
|
1.0
|
CA
|
A:ASN48
|
4.7
|
0.6
|
1.0
|
H
|
A:SER39
|
4.8
|
0.4
|
1.0
|
CB
|
A:ASP51
|
4.9
|
0.3
|
1.0
|
CG
|
A:LEU47
|
4.9
|
0.4
|
1.0
|
|
Reference:
W.J.Wu,
M.I.Su,
J.L.Wu,
S.Kumar,
L.H.Lim,
C.W.Wang,
F.H.Nelissen,
M.C.Chen,
J.F.Doreleijers,
S.S.Wijmenga,
M.D.Tsai.
How A Low-Fidelity Dna Polymerase Chooses Non-Watson-Crick From Watson-Crick Incorporation. J.Am.Chem.Soc. 2014.
ISSN: ESSN 1520-5126
PubMed: 24617852
DOI: 10.1021/JA4102375
Page generated: Wed Aug 14 00:51:43 2024
|