Sodium in PDB 2eid: Galactose Oxidase W290G Mutant

All present enzymatic activity of Galactose Oxidase W290G Mutant:
1.1.3.9;

The structure of Galactose Oxidase W290G Mutant, PDB code: 2eid was solved by S.E.Phillips, M.J.Mcpherson, P.F.Knowles, N.Akyumani, S.J.Firbank, S.Tamber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.20
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	89.884, 89.884, 415.325, 90.00, 90.00, 120.00
R / Rfree (%)	19.2 / 22.6

The structure of Galactose Oxidase W290G Mutant also contains other interesting chemical elements:

Copper

(Cu)

1 atom

The binding sites of Sodium atom in the Galactose Oxidase W290G Mutant (pdb code 2eid). 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 Galactose Oxidase W290G Mutant, PDB code: 2eid:

Sodium binding site 1 out of 1 in the Galactose Oxidase W290G Mutant


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Galactose Oxidase W290G Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Na641 b:1.0 occ:1.00 O A:ASN34 2.7 20.4 1.0 O A:ALA141 2.7 15.1 1.0 O A:LYS29 2.8 22.5 1.0 OD1 A:ASP32 2.8 19.5 1.0 O A:THR37 2.8 22.3 1.0 OE2 A:GLU142 2.8 16.2 1.0 OG1 A:THR37 2.9 23.8 1.0 C A:THR37 3.5 21.8 1.0 C A:LYS29 3.7 20.4 1.0 CG A:ASP32 3.7 18.8 1.0 C A:ALA141 3.8 13.6 1.0 C A:ASN34 3.8 19.8 1.0 OD2 A:ASP32 3.9 18.4 1.0 CB A:THR37 3.9 22.9 1.0 CD A:GLU142 3.9 15.5 1.0 CA A:THR37 4.1 22.8 1.0 CA A:ALA30 4.2 17.1 1.0 N A:THR37 4.2 23.2 1.0 N A:ALA30 4.3 18.8 1.0 N A:ASN34 4.3 17.6 1.0 N A:PHE38 4.4 20.8 1.0 CG A:GLU142 4.4 14.7 1.0 CA A:ASN34 4.4 18.7 1.0 CB A:ASN34 4.4 18.1 1.0 CA A:ALA141 4.4 12.8 1.0 C A:ALA30 4.6 17.1 1.0 CA A:LYS29 4.7 21.1 1.0 CA A:PHE38 4.7 18.6 1.0 N A:GLU142 4.8 14.7 1.0 N A:ASP32 4.9 17.8 1.0 N A:LYS35 4.9 21.0 1.0 N A:GLY33 4.9 16.6 1.0 N A:ILE31 4.9 17.3 1.0 O A:ALA30 5.0 16.1 1.0

M.S.Rogers, E.M.Tyler, N.Akyumani, C.R.Kurtis, R.K.Spooner, S.E.Deacon, S.Tamber, S.J.Firbank, K.Mahmoud, P.F.Knowles, S.E.Phillips, M.J.Mcpherson, D.M.Dooley. The Stacking Tryptophan of Galactose Oxidase: A Second-Coordination Sphere Residue That Has Profound Effects on Tyrosyl Radical Behavior and Enzyme Catalysis Biochemistry V. 46 4606 2007.
ISSN: ISSN 0006-2960
PubMed: 17385891
DOI: 10.1021/BI062139D