Atomistry » Magnesium » PDB 1xyl-1ydf » 1y07
Atomistry »
  Magnesium »
    PDB 1xyl-1ydf »
      1y07 »

Magnesium in PDB 1y07: Crystal Structure of the Superoxide Reductase From Treponema Pallidum

Enzymatic activity of Crystal Structure of the Superoxide Reductase From Treponema Pallidum

All present enzymatic activity of Crystal Structure of the Superoxide Reductase From Treponema Pallidum:
1.15.1.2;

Protein crystallography data

The structure of Crystal Structure of the Superoxide Reductase From Treponema Pallidum, PDB code: 1y07 was solved by T.Santos-Silva, J.Trincao, A.L.Carvalho, C.Bonifacio, F.Auchere, J.Moura, M.J.Romao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 63.25 / 1.55
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 119.311, 59.946, 65.520, 90.00, 104.96, 90.00
R / Rfree (%) 18.2 / 23.5

Other elements in 1y07:

The structure of Crystal Structure of the Superoxide Reductase From Treponema Pallidum also contains other interesting chemical elements:

Iron (Fe) 5 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Superoxide Reductase From Treponema Pallidum (pdb code 1y07). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Superoxide Reductase From Treponema Pallidum, PDB code: 1y07:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1y07

Go back to Magnesium Binding Sites List in 1y07
Magnesium binding site 1 out of 2 in the Crystal Structure of the Superoxide Reductase From Treponema Pallidum


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Superoxide Reductase From Treponema Pallidum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:10.2
occ:0.50
O A:HOH550 2.0 24.9 1.0
O A:ALA108 2.0 8.3 1.0
O A:HOH551 2.0 20.5 1.0
O C:HOH522 2.1 18.7 1.0
O A:HOH513 2.1 23.8 1.0
O C:HOH520 2.2 22.8 1.0
C A:ALA108 3.2 7.4 1.0
O C:HOH504 3.9 18.3 1.0
CA A:ALA108 4.0 7.7 1.0
O A:HOH567 4.2 28.6 1.0
O C:HOH512 4.2 23.4 1.0
N A:ASP109 4.2 8.9 1.0
O A:ASP110 4.2 6.7 1.0
O C:LYS128 4.3 11.8 1.0
O C:HOH552 4.3 36.3 1.0
O A:HOH552 4.4 25.5 1.0
CB A:ALA108 4.4 8.0 1.0
O C:VAL54 4.5 10.6 1.0
CA A:ASP109 4.5 8.7 1.0
C C:LYS128 4.5 10.0 1.0
C A:ASP109 4.8 8.4 1.0
O C:HOH588 4.9 41.3 1.0
N A:ASP110 4.9 8.0 1.0

Magnesium binding site 2 out of 2 in 1y07

Go back to Magnesium Binding Sites List in 1y07
Magnesium binding site 2 out of 2 in the Crystal Structure of the Superoxide Reductase From Treponema Pallidum


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Superoxide Reductase From Treponema Pallidum within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg502

b:20.7
occ:0.80
O C:HOH525 2.0 24.9 1.0
O A:HOH538 2.0 21.4 1.0
O C:HOH518 2.0 28.7 1.0
O C:ALA108 2.1 10.0 1.0
O C:HOH526 2.1 24.8 1.0
O C:HOH542 2.2 24.5 1.0
C C:ALA108 3.3 9.3 1.0
O A:HOH510 4.0 23.4 1.0
CA C:ALA108 4.0 9.3 1.0
O A:LYS128 4.0 12.4 1.0
O C:HOH546 4.0 36.1 1.0
O A:HOH524 4.2 26.5 1.0
N C:ASP109 4.3 11.0 1.0
O C:ASP110 4.4 6.8 1.0
O C:HOH591 4.4 32.0 1.0
O A:HOH564 4.4 27.5 1.0
CB C:ALA108 4.4 9.7 1.0
O A:VAL54 4.5 10.9 1.0
C A:LYS128 4.5 13.6 1.0
O C:HOH543 4.5 31.0 1.0
CA C:ASP109 4.5 9.8 1.0
C C:ASP109 4.8 10.4 1.0
CE1 C:HIS59 4.9 29.9 1.0
N C:ASP110 4.9 9.2 1.0

Reference:

T.Santos-Silva, J.Trincao, A.L.Carvalho, C.Bonifacio, F.Auchere, P.Raleiras, I.Moura, J.Moura, M.J.Romao. The First Crystal Structure of Class III Superoxide Reductase From Treponema Pallidum. J.Biol.Inorg.Chem. V. 11 548 2006.
ISSN: ISSN 0949-8257
PubMed: 16791639
DOI: 10.1007/S00775-006-0104-Y
Page generated: Tue Aug 13 18:27:58 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy