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Sodium in PDB 1saz: Membership in the Askha Superfamily: Enzymological Properties and Crystal Structure of Butyrate Kinase 2 From Thermotoga Maritima

Enzymatic activity of Membership in the Askha Superfamily: Enzymological Properties and Crystal Structure of Butyrate Kinase 2 From Thermotoga Maritima

All present enzymatic activity of Membership in the Askha Superfamily: Enzymological Properties and Crystal Structure of Butyrate Kinase 2 From Thermotoga Maritima:
2.7.2.7;

Protein crystallography data

The structure of Membership in the Askha Superfamily: Enzymological Properties and Crystal Structure of Butyrate Kinase 2 From Thermotoga Maritima, PDB code: 1saz was solved by J.Diao, D.R.Cooper, D.A.Sanders, M.S.Hasson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.64 / 2.50
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 197.685, 197.685, 58.238, 90.00, 90.00, 90.00
R / Rfree (%) 21.7 / 26.7

Sodium Binding Sites:

The binding sites of Sodium atom in the Membership in the Askha Superfamily: Enzymological Properties and Crystal Structure of Butyrate Kinase 2 From Thermotoga Maritima (pdb code 1saz). 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 Membership in the Askha Superfamily: Enzymological Properties and Crystal Structure of Butyrate Kinase 2 From Thermotoga Maritima, PDB code: 1saz:

Sodium binding site 1 out of 1 in 1saz

Go back to Sodium Binding Sites List in 1saz
Sodium binding site 1 out of 1 in the Membership in the Askha Superfamily: Enzymological Properties and Crystal Structure of Butyrate Kinase 2 From Thermotoga Maritima


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Membership in the Askha Superfamily: Enzymological Properties and Crystal Structure of Butyrate Kinase 2 From Thermotoga Maritima within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na390

b:36.6
occ:1.00
 O A:SER215 2.3 36.2 1.0
O A:THR217 2.4 31.8 1.0
C A:GLY216 3.3 35.3 1.0
C A:THR217 3.4 32.8 1.0
C A:SER215 3.5 36.4 1.0
N A:THR217 3.5 34.6 1.0
O A:GLY216 3.6 38.5 1.0
CA A:GLY216 3.7 35.5 1.0
CB A:PHE210 3.8 25.9 1.0
CA A:THR217 4.0 33.7 1.0
N A:GLY216 4.1 36.4 1.0
OE1 A:GLN280 4.1 31.4 1.0
N A:PHE210 4.2 27.4 1.0
O A:GLY208 4.2 31.3 1.0
CD2 A:LEU218 4.3 36.2 1.0
CA A:PHE210 4.4 29.6 1.0
NE2 A:GLN280 4.5 29.1 1.0
N A:LEU218 4.5 33.6 1.0
CB A:THR217 4.6 34.2 1.0
CA A:SER215 4.7 36.5 1.0
CD A:GLN280 4.7 27.5 1.0
CD2 A:PHE210 4.7 25.0 1.0
C A:PRO209 4.8 26.6 1.0
CG A:PHE210 4.8 25.2 1.0
CG A:LEU218 4.9 36.3 1.0
CA A:LEU218 4.9 34.7 1.0

Reference:

J.Diao, M.S.Hasson. Crystal Structure of Butyrate Kinase 2 From Thermotoga Maritima, A Member of the Askha Superfamily of Phosphotransferases. J.Bacteriol. V. 191 2521 2009.
ISSN: ISSN 0021-9193
PubMed: 19201797
DOI: 10.1128/JB.00906-08
Page generated: Sun Oct 6 22:23:31 2024

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