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Sodium in PDB 8cgs: Crystal Structure of Arsenite Oxidase From Alcaligenes Faecalis (Af Aio) Bound to Antimony Oxyanion

Enzymatic activity of Crystal Structure of Arsenite Oxidase From Alcaligenes Faecalis (Af Aio) Bound to Antimony Oxyanion

All present enzymatic activity of Crystal Structure of Arsenite Oxidase From Alcaligenes Faecalis (Af Aio) Bound to Antimony Oxyanion:
1.20.9.1;

Protein crystallography data

The structure of Crystal Structure of Arsenite Oxidase From Alcaligenes Faecalis (Af Aio) Bound to Antimony Oxyanion, PDB code: 8cgs was solved by F.Engrola, M.A.S.Correia, M.J.Romao, T.Santos-Silva, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 116.27 / 1.84
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 90.378, 109.21, 117.342, 97.71, 90.06, 96.28
R / Rfree (%) 15.4 / 18.9

Other elements in 8cgs:

The structure of Crystal Structure of Arsenite Oxidase From Alcaligenes Faecalis (Af Aio) Bound to Antimony Oxyanion also contains other interesting chemical elements:

Chlorine (Cl) 5 atoms
Iron (Fe) 20 atoms
Molybdenum (Mo) 4 atoms
Antimony (Sb) 4 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Arsenite Oxidase From Alcaligenes Faecalis (Af Aio) Bound to Antimony Oxyanion (pdb code 8cgs). 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 Crystal Structure of Arsenite Oxidase From Alcaligenes Faecalis (Af Aio) Bound to Antimony Oxyanion, PDB code: 8cgs:

Sodium binding site 1 out of 1 in 8cgs

Go back to Sodium Binding Sites List in 8cgs
Sodium binding site 1 out of 1 in the Crystal Structure of Arsenite Oxidase From Alcaligenes Faecalis (Af Aio) Bound to Antimony Oxyanion


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Arsenite Oxidase From Alcaligenes Faecalis (Af Aio) Bound to Antimony Oxyanion within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Na5012

b:32.8
occ:1.00
 O G:HOH5505 2.6 28.4 1.0
OH G:TYR110 2.7 17.5 1.0
O G:LYS117 2.8 16.4 1.0
NZ G:LYS121 3.4 40.7 1.0
O G:HOH5319 3.5 32.5 1.0
CZ G:TYR110 3.6 18.1 1.0
CE1 G:TYR110 3.7 16.3 1.0
CD G:LYS121 3.8 35.5 1.0
C G:LYS117 3.8 15.0 1.0
CA G:PRO112 3.9 17.6 1.0
CA G:LYS117 4.0 15.3 1.0
CE G:LYS121 4.1 40.1 1.0
O G:PRO112 4.1 17.8 1.0
CG G:LYS117 4.3 19.5 1.0
CB G:PRO112 4.4 17.4 1.0
C G:PRO112 4.4 16.8 1.0
CG G:LYS121 4.6 31.5 1.0
O G:THR111 4.6 17.8 1.0
O G:HOH5175 4.7 29.8 1.0
CB G:LYS117 4.7 17.1 1.0
N G:PRO112 4.9 17.5 1.0
O G:GLY116 4.9 14.4 1.0
CE2 G:TYR110 4.9 18.8 1.0
N G:GLN118 5.0 14.2 1.0
CD1 G:TYR110 5.0 15.4 1.0

Reference:

F.Engrola, M.A.S.Correia, M.J.Romao, T.Santos-Silva. Arsenite Oxidase in Complex with Antimonite and Arsenite Oxyanions - Insights Into the Catalytic Mechanism To Be Published.
Page generated: Wed Oct 9 10:55:27 2024

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