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Sodium in PDB 7ule: F420-1/Gdp Complex of F420-Gamma Glutamyl Ligase (Cofe) From Archaeoglobus Fulgidus

Enzymatic activity of F420-1/Gdp Complex of F420-Gamma Glutamyl Ligase (Cofe) From Archaeoglobus Fulgidus

All present enzymatic activity of F420-1/Gdp Complex of F420-Gamma Glutamyl Ligase (Cofe) From Archaeoglobus Fulgidus:
6.3.2.31; 6.3.2.34;

Protein crystallography data

The structure of F420-1/Gdp Complex of F420-Gamma Glutamyl Ligase (Cofe) From Archaeoglobus Fulgidus, PDB code: 7ule was solved by G.Bashiri, C.J.Squire, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.90 / 1.70
Space group P 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 69.082, 69.082, 92.352, 90, 90, 90
R / Rfree (%) 21 / 23.4

Other elements in 7ule:

The structure of F420-1/Gdp Complex of F420-Gamma Glutamyl Ligase (Cofe) From Archaeoglobus Fulgidus also contains other interesting chemical elements:

Manganese (Mn) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the F420-1/Gdp Complex of F420-Gamma Glutamyl Ligase (Cofe) From Archaeoglobus Fulgidus (pdb code 7ule). 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 F420-1/Gdp Complex of F420-Gamma Glutamyl Ligase (Cofe) From Archaeoglobus Fulgidus, PDB code: 7ule:

Sodium binding site 1 out of 1 in 7ule

Go back to Sodium Binding Sites List in 7ule
Sodium binding site 1 out of 1 in the F420-1/Gdp Complex of F420-Gamma Glutamyl Ligase (Cofe) From Archaeoglobus Fulgidus


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of F420-1/Gdp Complex of F420-Gamma Glutamyl Ligase (Cofe) From Archaeoglobus Fulgidus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na305

b:37.3
occ:1.00
 O A:HOH452 2.3 36.0 1.0
O A:HOH463 2.3 40.2 1.0
OD1 A:ASP109 2.3 36.2 1.0
O2P A:F4I302 2.3 37.0 1.0
O A:HOH446 2.3 38.1 1.0
O A:HOH401 2.8 34.8 1.0
CG A:ASP109 3.3 35.8 1.0
OD2 A:ASP109 3.6 36.3 1.0
P A:F4I302 3.7 37.4 1.0
MN A:MN304 3.7 33.0 1.0
C3I A:F4I302 3.8 37.1 1.0
O3I A:F4I302 3.9 35.6 1.0
O A:HOH450 4.0 46.1 1.0
O A:THR151 4.0 26.4 1.0
CA A:GLY107 4.1 32.7 1.0
O3P A:F4I302 4.2 34.7 1.0
N A:F4I302 4.2 36.9 1.0
C A:GLY107 4.2 33.4 1.0
O A:GLY107 4.2 32.2 1.0
O A:VAL104 4.3 31.3 1.0
O A:ILE108 4.4 33.4 1.0
O1P A:F4I302 4.4 37.3 1.0
C1I A:F4I302 4.4 36.9 1.0
OD2 A:ASP150 4.4 29.5 1.0
OD1 A:ASP150 4.5 30.9 1.0
O A:HOH412 4.6 43.4 1.0
CB A:ASP109 4.7 35.2 1.0
CA A:F4I302 4.7 38.3 1.0
C A:ILE108 4.8 34.0 1.0
O5' A:F4I302 4.8 37.0 1.0
CG A:ASP150 4.9 27.6 1.0
N A:ILE108 4.9 33.0 1.0
N A:GLY107 4.9 32.4 1.0
CA A:ASP109 4.9 35.0 1.0

Reference:

G.Bashiri, W.Bramley, E.Bulloch, S.Stutely, M.Middleditch, P.Young, M.Naqvi, P.Harris, E.N.Baker, C.J.Squire. A Universal Mechanism For Poly-Glutamylation To Be Published.
Page generated: Wed Oct 9 09:15:13 2024

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