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Sodium in PDB 2eib: Crystal Structure of Galactose Oxidase, W290H Mutant

Enzymatic activity of Crystal Structure of Galactose Oxidase, W290H Mutant

All present enzymatic activity of Crystal Structure of Galactose Oxidase, W290H Mutant:
1.1.3.9;

Protein crystallography data

The structure of Crystal Structure of Galactose Oxidase, W290H Mutant, PDB code: 2eib was solved by S.E.Phillips, M.J.Mcpherson, P.F.Knowles, C.Wilmot, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 98.000, 89.400, 86.700, 90.00, 117.80, 90.00
R / Rfree (%) n/a / n/a

Other elements in 2eib:

The structure of Crystal Structure of Galactose Oxidase, W290H Mutant also contains other interesting chemical elements:

Copper (Cu) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Galactose Oxidase, W290H Mutant (pdb code 2eib). 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 Galactose Oxidase, W290H Mutant, PDB code: 2eib:

Sodium binding site 1 out of 1 in 2eib

Go back to Sodium Binding Sites List in 2eib
Sodium binding site 1 out of 1 in the Crystal Structure of Galactose Oxidase, W290H Mutant


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 Galactose Oxidase, W290H Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na702

b:18.6
occ:1.00
O A:LYS29 2.1 22.3 1.0
O A:ASN34 2.4 47.4 1.0
OG1 A:THR37 2.4 30.6 1.0
O A:ALA141 2.5 35.1 1.0
OD1 A:ASP32 2.5 30.1 1.0
O A:THR37 2.6 25.3 1.0
OE2 A:GLU142 2.8 37.0 1.0
C A:THR37 3.2 33.4 1.0
C A:LYS29 3.3 23.0 1.0
CG A:ASP32 3.4 37.5 1.0
OD2 A:ASP32 3.5 40.8 1.0
CB A:THR37 3.5 48.5 1.0
C A:ASN34 3.5 38.1 1.0
C A:ALA141 3.6 21.6 1.0
CA A:THR37 3.7 40.2 1.0
CD A:GLU142 3.9 30.9 1.0
N A:THR37 3.9 43.0 1.0
N A:ASN34 4.1 49.3 1.0
N A:PHE38 4.1 32.3 1.0
CA A:LYS29 4.2 21.9 1.0
N A:ALA30 4.2 22.7 1.0
CA A:ASN34 4.3 39.4 1.0
CA A:ALA30 4.3 19.0 1.0
CA A:ALA141 4.4 16.4 1.0
CB A:LYS29 4.4 33.0 1.0
N A:GLU142 4.4 22.6 1.0
N A:LYS35 4.5 41.8 1.0
C A:ALA30 4.6 25.6 1.0
CG A:GLU142 4.6 27.8 1.0
CA A:PHE38 4.6 31.9 1.0
N A:ASP32 4.6 60.9 1.0
CB A:ASN34 4.6 60.4 1.0
O A:ALA30 4.7 23.7 1.0
CB A:ASP32 4.7 46.8 1.0
CA A:GLU142 4.8 19.5 1.0
N A:GLY33 4.8 61.3 1.0
OE1 A:GLU142 4.8 45.9 1.0
CG2 A:THR37 4.9 62.2 1.0
CA A:LYS35 4.9 45.2 1.0
N A:ASP36 5.0 50.0 1.0

Reference:

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
Page generated: Tue Dec 15 05:48:04 2020

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