Atomistry » Magnesium » PDB 7tr3-7u0r » 7tu8
Atomistry »
  Magnesium »
    PDB 7tr3-7u0r »
      7tu8 »

Magnesium in PDB 7tu8: Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp

Enzymatic activity of Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp

All present enzymatic activity of Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp:
3.1.5.1;

Magnesium Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Magnesium atom in the Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp (pdb code 7tu8). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 12 binding sites of Magnesium where determined in the Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp, PDB code: 7tu8:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 12 in 7tu8

Go back to Magnesium Binding Sites List in 7tu8
Magnesium binding site 1 out of 12 in the Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg503

b:34.6
occ:1.00
 NE2 A:HIS116 1.9 45.3 1.0
NE2 A:HIS68 2.0 45.3 1.0
OD1 A:ASP117 2.2 45.3 1.0
OD1 A:ASP253 2.4 45.3 1.0
CE1 A:HIS116 2.6 45.3 1.0
CE1 A:HIS68 3.0 45.3 1.0
CD2 A:HIS68 3.0 45.3 1.0
CD2 A:HIS116 3.1 45.3 1.0
CG A:ASP117 3.1 45.3 1.0
CG A:ASP253 3.4 45.3 1.0
OD2 A:ASP117 3.5 45.3 1.0
ND1 A:HIS116 3.8 45.3 1.0
OD2 A:ASP253 3.9 45.3 1.0
CG A:HIS116 4.0 45.3 1.0
ND1 A:HIS68 4.1 45.3 1.0
CG A:HIS68 4.1 45.3 1.0
O1A A:DGT501 4.2 46.2 1.0
NH1 A:ARG65 4.3 45.3 1.0
CB A:ASP117 4.4 45.3 1.0
CB A:ASP253 4.5 45.3 1.0
CG2 A:VAL72 4.9 45.3 1.0

Magnesium binding site 2 out of 12 in 7tu8

Go back to Magnesium Binding Sites List in 7tu8
Magnesium binding site 2 out of 12 in the Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg504

b:43.4
occ:1.00
 O1G A:DTP502 2.2 42.5 1.0
O2B A:DTP502 2.8 42.5 1.0
O2A A:DTP502 2.8 42.5 1.0
O3A A:DTP502 3.0 42.5 1.0
O3B A:DTP502 3.0 42.5 1.0
PG A:DTP502 3.2 42.5 1.0
PB A:DTP502 3.2 42.5 1.0
PA A:DTP502 3.6 42.5 1.0
O2G A:DTP502 4.2 42.5 1.0
O3G A:DTP502 4.2 42.5 1.0
N7 A:DTP502 4.5 42.5 1.0
O5' A:DTP502 4.5 42.5 1.0
NH1 A:ARG28 4.6 45.3 1.0
O1B A:DTP502 4.7 42.5 1.0
O B:ALA308 4.7 45.3 1.0
O1A A:DTP502 4.7 42.5 1.0
C8 A:DTP502 4.8 42.5 1.0

Magnesium binding site 3 out of 12 in 7tu8

Go back to Magnesium Binding Sites List in 7tu8
Magnesium binding site 3 out of 12 in the Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg505

b:43.4
occ:1.00
 O1G B:DTP502 2.2 42.5 1.0
O2B B:DTP502 2.8 42.5 1.0
O2A B:DTP502 2.8 42.5 1.0
O3A B:DTP502 3.0 42.5 1.0
O3B B:DTP502 3.0 42.5 1.0
PG B:DTP502 3.2 42.5 1.0
PB B:DTP502 3.2 42.5 1.0
PA B:DTP502 3.6 42.5 1.0
O2G B:DTP502 4.2 42.5 1.0
O3G B:DTP502 4.2 42.5 1.0
N7 B:DTP502 4.5 42.5 1.0
O5' B:DTP502 4.5 42.5 1.0
NH1 B:ARG28 4.6 45.3 1.0
O A:ALA308 4.6 45.3 1.0
O1B B:DTP502 4.7 42.5 1.0
O1A B:DTP502 4.7 42.5 1.0
C8 B:DTP502 4.8 42.5 1.0

Magnesium binding site 4 out of 12 in 7tu8

Go back to Magnesium Binding Sites List in 7tu8
Magnesium binding site 4 out of 12 in the Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg503

b:34.6
occ:1.00
 NE2 B:HIS116 1.9 45.3 1.0
NE2 B:HIS68 2.0 45.3 1.0
OD1 B:ASP117 2.2 45.3 1.0
OD1 B:ASP253 2.4 45.3 1.0
CE1 B:HIS116 2.6 45.3 1.0
CE1 B:HIS68 3.0 45.3 1.0
CD2 B:HIS68 3.0 45.3 1.0
CD2 B:HIS116 3.1 45.3 1.0
CG B:ASP117 3.1 45.3 1.0
CG B:ASP253 3.4 45.3 1.0
OD2 B:ASP117 3.5 45.3 1.0
ND1 B:HIS116 3.8 45.3 1.0
OD2 B:ASP253 3.9 45.3 1.0
CG B:HIS116 4.0 45.3 1.0
ND1 B:HIS68 4.1 45.3 1.0
CG B:HIS68 4.1 45.3 1.0
O1A B:DGT501 4.2 46.2 1.0
NH1 B:ARG65 4.3 45.3 1.0
CB B:ASP117 4.4 45.3 1.0
CB B:ASP253 4.5 45.3 1.0
CG2 B:VAL72 4.9 45.3 1.0

Magnesium binding site 5 out of 12 in 7tu8

Go back to Magnesium Binding Sites List in 7tu8
Magnesium binding site 5 out of 12 in the Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg503

b:34.6
occ:1.00
 NE2 C:HIS116 1.9 45.3 1.0
NE2 C:HIS68 2.0 45.3 1.0
OD1 C:ASP117 2.2 45.3 1.0
OD1 C:ASP253 2.4 45.3 1.0
CE1 C:HIS116 2.6 45.3 1.0
CE1 C:HIS68 3.0 45.3 1.0
CD2 C:HIS68 3.0 45.3 1.0
CD2 C:HIS116 3.1 45.3 1.0
CG C:ASP117 3.1 45.3 1.0
CG C:ASP253 3.4 45.3 1.0
OD2 C:ASP117 3.5 45.3 1.0
ND1 C:HIS116 3.8 45.3 1.0
OD2 C:ASP253 3.9 45.3 1.0
CG C:HIS116 4.0 45.3 1.0
ND1 C:HIS68 4.1 45.3 1.0
CG C:HIS68 4.1 45.3 1.0
O1A C:DGT501 4.2 46.2 1.0
NH1 C:ARG65 4.3 45.3 1.0
CB C:ASP117 4.4 45.3 1.0
CB C:ASP253 4.5 45.3 1.0
CG2 C:VAL72 4.9 45.3 1.0

Magnesium binding site 6 out of 12 in 7tu8

Go back to Magnesium Binding Sites List in 7tu8
Magnesium binding site 6 out of 12 in the Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg504

b:43.4
occ:1.00
 O1G C:DTP502 2.2 42.5 1.0
O2B C:DTP502 2.8 42.5 1.0
O2A C:DTP502 2.8 42.5 1.0
O3A C:DTP502 3.0 42.5 1.0
O3B C:DTP502 3.0 42.5 1.0
PG C:DTP502 3.2 42.5 1.0
PB C:DTP502 3.2 42.5 1.0
PA C:DTP502 3.6 42.5 1.0
O2G C:DTP502 4.2 42.5 1.0
O3G C:DTP502 4.2 42.5 1.0
N7 C:DTP502 4.5 42.5 1.0
O5' C:DTP502 4.5 42.5 1.0
NH1 C:ARG28 4.6 45.3 1.0
O D:ALA308 4.7 45.3 1.0
O1B C:DTP502 4.7 42.5 1.0
O1A C:DTP502 4.7 42.5 1.0
C8 C:DTP502 4.8 42.5 1.0

Magnesium binding site 7 out of 12 in 7tu8

Go back to Magnesium Binding Sites List in 7tu8
Magnesium binding site 7 out of 12 in the Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg505

b:43.4
occ:1.00
 O1G D:DTP502 2.2 42.5 1.0
O2B D:DTP502 2.8 42.5 1.0
O2A D:DTP502 2.8 42.5 1.0
O3A D:DTP502 3.0 42.5 1.0
O3B D:DTP502 3.0 42.5 1.0
PG D:DTP502 3.2 42.5 1.0
PB D:DTP502 3.2 42.5 1.0
PA D:DTP502 3.6 42.5 1.0
O2G D:DTP502 4.2 42.5 1.0
O3G D:DTP502 4.2 42.5 1.0
N7 D:DTP502 4.5 42.5 1.0
O5' D:DTP502 4.5 42.5 1.0
NH1 D:ARG28 4.6 45.3 1.0
O1B D:DTP502 4.7 42.5 1.0
O C:ALA308 4.7 45.3 1.0
O1A D:DTP502 4.7 42.5 1.0
C8 D:DTP502 4.8 42.5 1.0

Magnesium binding site 8 out of 12 in 7tu8

Go back to Magnesium Binding Sites List in 7tu8
Magnesium binding site 8 out of 12 in the Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 8 of Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg503

b:34.6
occ:1.00
 NE2 D:HIS116 1.9 45.3 1.0
NE2 D:HIS68 2.0 45.3 1.0
OD1 D:ASP117 2.2 45.3 1.0
OD1 D:ASP253 2.4 45.3 1.0
CE1 D:HIS116 2.6 45.3 1.0
CE1 D:HIS68 3.0 45.3 1.0
CD2 D:HIS68 3.0 45.3 1.0
CD2 D:HIS116 3.1 45.3 1.0
CG D:ASP117 3.1 45.3 1.0
CG D:ASP253 3.4 45.3 1.0
OD2 D:ASP117 3.5 45.3 1.0
ND1 D:HIS116 3.8 45.3 1.0
OD2 D:ASP253 3.9 45.3 1.0
CG D:HIS116 4.0 45.3 1.0
ND1 D:HIS68 4.1 45.3 1.0
CG D:HIS68 4.1 45.3 1.0
O1A D:DGT501 4.2 46.2 1.0
NH1 D:ARG65 4.3 45.3 1.0
CB D:ASP117 4.4 45.3 1.0
CB D:ASP253 4.5 45.3 1.0
CG2 D:VAL72 4.9 45.3 1.0

Magnesium binding site 9 out of 12 in 7tu8

Go back to Magnesium Binding Sites List in 7tu8
Magnesium binding site 9 out of 12 in the Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 9 of Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg503

b:34.6
occ:1.00
 NE2 E:HIS116 1.9 45.3 1.0
NE2 E:HIS68 2.0 45.3 1.0
OD1 E:ASP117 2.2 45.3 1.0
OD1 E:ASP253 2.4 45.3 1.0
CE1 E:HIS116 2.6 45.3 1.0
CE1 E:HIS68 3.0 45.3 1.0
CD2 E:HIS68 3.0 45.3 1.0
CD2 E:HIS116 3.1 45.3 1.0
CG E:ASP117 3.1 45.3 1.0
CG E:ASP253 3.4 45.3 1.0
OD2 E:ASP117 3.5 45.3 1.0
ND1 E:HIS116 3.8 45.3 1.0
OD2 E:ASP253 3.9 45.3 1.0
CG E:HIS116 4.0 45.3 1.0
ND1 E:HIS68 4.1 45.3 1.0
CG E:HIS68 4.1 45.3 1.0
O1A E:DGT501 4.2 46.2 1.0
NH1 E:ARG65 4.3 45.3 1.0
CB E:ASP117 4.4 45.3 1.0
CB E:ASP253 4.5 45.3 1.0
CG2 E:VAL72 4.9 45.3 1.0

Magnesium binding site 10 out of 12 in 7tu8

Go back to Magnesium Binding Sites List in 7tu8
Magnesium binding site 10 out of 12 in the Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 10 of Structure of the L. Blandensis Dgtpase H125A Mutant Bound to Dgtp and Datp within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg504

b:43.4
occ:1.00
 O1G E:DTP502 2.2 42.5 1.0
O2B E:DTP502 2.8 42.5 1.0
O2A E:DTP502 2.8 42.5 1.0
O3A E:DTP502 3.0 42.5 1.0
O3B E:DTP502 3.0 42.5 1.0
PG E:DTP502 3.2 42.5 1.0
PB E:DTP502 3.2 42.5 1.0
PA E:DTP502 3.6 42.5 1.0
O2G E:DTP502 4.2 42.5 1.0
O3G E:DTP502 4.2 42.5 1.0
N7 E:DTP502 4.5 42.5 1.0
O5' E:DTP502 4.5 42.5 1.0
NH1 E:ARG28 4.6 45.3 1.0
O F:ALA308 4.6 45.3 1.0
O1B E:DTP502 4.7 42.5 1.0
O1A E:DTP502 4.7 42.5 1.0
C8 E:DTP502 4.8 42.5 1.0

Reference:

B.P.Klemm, A.P.Sikkema, A.L.Hsu, J.C.Horng, T.M.T.Hall, M.J.Borgnia, R.M.Schaaper. High-Resolution Structures of the SAMHD1 Dgtpase Homolog From Leeuwenhoekiella Blandensis Reveal A Novel Mechanism of Allosteric Activation By Datp. J.Biol.Chem. V. 298 02073 2022.
ISSN: ESSN 1083-351X
PubMed: 35643313
DOI: 10.1016/J.JBC.2022.102073
Page generated: Thu Oct 3 09:29:36 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy