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Sodium in PDB 3mua: Enzyme-Substrate Interactions of IXT6, the Intracellular Xylanase of G. Stearothermophilus.

Enzymatic activity of Enzyme-Substrate Interactions of IXT6, the Intracellular Xylanase of G. Stearothermophilus.

All present enzymatic activity of Enzyme-Substrate Interactions of IXT6, the Intracellular Xylanase of G. Stearothermophilus.:
3.2.1.8;

Protein crystallography data

The structure of Enzyme-Substrate Interactions of IXT6, the Intracellular Xylanase of G. Stearothermophilus., PDB code: 3mua was solved by V.Solomon, G.Zolotnitsky, R.Alhadeff, Y.Shoham, G.Shoham, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.56 / 1.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 169.228, 80.771, 79.056, 90.00, 91.73, 90.00
R / Rfree (%) 19.2 / 20.2

Sodium Binding Sites:

The binding sites of Sodium atom in the Enzyme-Substrate Interactions of IXT6, the Intracellular Xylanase of G. Stearothermophilus. (pdb code 3mua). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Enzyme-Substrate Interactions of IXT6, the Intracellular Xylanase of G. Stearothermophilus., PDB code: 3mua:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 3mua

Go back to Sodium Binding Sites List in 3mua
Sodium binding site 1 out of 2 in the Enzyme-Substrate Interactions of IXT6, the Intracellular Xylanase of G. Stearothermophilus.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Enzyme-Substrate Interactions of IXT6, the Intracellular Xylanase of G. Stearothermophilus. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na401

b:20.7
occ:1.00
O A:ARG282 2.2 20.1 1.0
O A:ASP15 2.2 20.1 1.0
O A:ILE285 2.4 17.7 1.0
OE1 A:GLN286 2.5 29.9 1.0
O A:HOH502 2.5 29.2 1.0
CD A:GLN286 3.1 28.4 1.0
NE2 A:GLN286 3.3 28.5 1.0
C A:ARG282 3.3 20.9 1.0
C A:ASP15 3.4 20.2 1.0
C A:ILE285 3.5 17.4 1.0
CA A:GLN286 3.9 17.9 1.0
CA A:ARG282 3.9 20.6 1.0
O A:HOH1070 4.0 46.6 1.0
N A:GLN286 4.1 17.2 1.0
CB A:ARG282 4.2 22.2 1.0
CA A:ASP15 4.3 20.8 1.0
CG A:GLN286 4.4 24.0 1.0
N A:PHE16 4.4 19.8 1.0
CB A:PHE16 4.4 18.4 1.0
N A:ASP283 4.4 22.1 1.0
CA A:PHE16 4.5 18.3 1.0
O A:HOH892 4.5 35.5 1.0
N A:ILE285 4.6 18.8 1.0
CB A:GLN286 4.6 20.1 1.0
CA A:ILE285 4.7 17.4 1.0
CA A:ASP283 4.7 23.3 1.0
CD2 A:PHE16 4.7 18.0 1.0
C A:ASP283 4.8 22.5 1.0
C A:GLN286 4.8 17.2 1.0
N A:VAL284 5.0 22.0 0.4
O A:HOH1044 5.0 40.0 1.0
N A:VAL284 5.0 21.7 0.6

Sodium binding site 2 out of 2 in 3mua

Go back to Sodium Binding Sites List in 3mua
Sodium binding site 2 out of 2 in the Enzyme-Substrate Interactions of IXT6, the Intracellular Xylanase of G. Stearothermophilus.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Enzyme-Substrate Interactions of IXT6, the Intracellular Xylanase of G. Stearothermophilus. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na402

b:25.0
occ:1.00
O B:ARG282 2.2 29.0 1.0
O B:ASP15 2.2 21.6 1.0
O B:ILE285 2.4 22.0 1.0
O B:HOH720 2.5 31.5 1.0
OE1 B:GLN286 2.8 30.6 0.6
NE2 B:GLN286 3.1 29.6 0.6
CD B:GLN286 3.2 28.8 0.6
C B:ARG282 3.3 29.5 1.0
C B:ASP15 3.4 21.7 1.0
C B:ILE285 3.5 22.6 1.0
CA B:ARG282 3.9 29.0 1.0
CA B:GLN286 3.9 21.7 0.6
CA B:GLN286 4.0 21.3 0.4
N B:GLN286 4.2 21.6 0.6
N B:GLN286 4.2 21.6 0.4
NE2 B:GLN286 4.2 27.7 0.4
CA B:ASP15 4.2 23.8 1.0
CB B:ARG282 4.2 29.6 1.0
N B:PHE16 4.4 20.4 1.0
CG B:GLN286 4.4 26.7 0.6
N B:ASP283 4.4 30.3 1.0
CB B:PHE16 4.4 19.5 1.0
CA B:PHE16 4.5 20.0 1.0
O B:HOH957 4.5 41.0 1.0
N B:ILE285 4.6 26.2 1.0
CG B:GLN286 4.6 25.0 0.4
CA B:ILE285 4.7 23.5 1.0
CB B:GLN286 4.7 23.5 0.6
CA B:ASP283 4.7 31.6 1.0
CD B:GLN286 4.7 26.1 0.4
CD2 B:PHE16 4.8 19.9 1.0
CB B:GLN286 4.8 22.6 0.4
C B:ASP283 4.8 31.7 1.0
C B:GLN286 4.9 20.4 0.6
C B:GLN286 4.9 20.2 0.4

Reference:

V.Solomon, G.Zolotnitsky, R.Alhadeff, Y.Shoham, G.Shoham. Enzyme-Substrate Interactions of IXT6, the Intracellular Xylanase of G. Stearothermophilus. To Be Published.
Page generated: Tue Dec 15 06:18:14 2020

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