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Sodium in PDB 1yf1: Structural and Biochemical Analysis of the Link Between Enzymatic Activity and Oligomerization in Ahpc, A Bacterial Peroxiredoxin.

Enzymatic activity of Structural and Biochemical Analysis of the Link Between Enzymatic Activity and Oligomerization in Ahpc, A Bacterial Peroxiredoxin.

All present enzymatic activity of Structural and Biochemical Analysis of the Link Between Enzymatic Activity and Oligomerization in Ahpc, A Bacterial Peroxiredoxin.:
1.11.1.15;

Protein crystallography data

The structure of Structural and Biochemical Analysis of the Link Between Enzymatic Activity and Oligomerization in Ahpc, A Bacterial Peroxiredoxin., PDB code: 1yf1 was solved by D.Parsonage, D.S.Youngblood, G.N.Sarma, Z.A.Wood, P.A.Karplus, L.B.Poole, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 100.00 / 2.60
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 136.350, 169.960, 117.650, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 23.7

Sodium Binding Sites:

The binding sites of Sodium atom in the Structural and Biochemical Analysis of the Link Between Enzymatic Activity and Oligomerization in Ahpc, A Bacterial Peroxiredoxin. (pdb code 1yf1). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Structural and Biochemical Analysis of the Link Between Enzymatic Activity and Oligomerization in Ahpc, A Bacterial Peroxiredoxin., PDB code: 1yf1:

Sodium binding site 1 out of 1 in 1yf1

Go back to Sodium Binding Sites List in 1yf1
Sodium binding site 1 out of 1 in the Structural and Biochemical Analysis of the Link Between Enzymatic Activity and Oligomerization in Ahpc, A Bacterial Peroxiredoxin.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structural and Biochemical Analysis of the Link Between Enzymatic Activity and Oligomerization in Ahpc, A Bacterial Peroxiredoxin. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na6001

b:14.8
occ:0.50
 O A:HOH1218 2.4 21.5 1.0
O A:HOH1076 2.6 23.6 1.0
O A:THR72 3.1 34.3 1.0
O A:PRO99 3.9 23.0 1.0
CA A:PRO99 4.2 21.6 1.0
O A:HOH1038 4.2 23.7 1.0
C A:THR72 4.2 30.4 1.0
CB A:THR72 4.3 26.3 1.0
OG1 A:THR72 4.3 24.3 1.0
C A:PRO99 4.5 22.6 1.0
CB A:PRO99 4.5 25.1 1.0
CA A:THR72 4.9 23.6 1.0
O A:GLY115 4.9 21.0 1.0
O A:HOH1250 5.0 26.8 1.0

Reference:

D.Parsonage, D.S.Youngblood, G.N.Sarma, Z.A.Wood, P.A.Karplus, L.B.Poole. Analysis of the Link Between Enzymatic Activity and Oligomeric State in Ahpc, A Bacterial Peroxiredoxin. Biochemistry V. 44 10583 2005.
ISSN: ISSN 0006-2960
PubMed: 16060667
DOI: 10.1021/BI050448I
Page generated: Mon Oct 7 00:40:26 2024

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