Sodium in PDB 7uld: Gtp Complex of F420-Gamma Glutamyl Ligase (Cofe) From Archaeoglobus Fulgidus

Enzymatic activity of Gtp Complex of F420-Gamma Glutamyl Ligase (Cofe) From Archaeoglobus Fulgidus

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

Protein crystallography data

The structure of Gtp Complex of F420-Gamma Glutamyl Ligase (Cofe) From Archaeoglobus Fulgidus, PDB code: 7uld 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) 43.04 / 1.30
Space group P 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 68.544, 68.544, 93.243, 90, 90, 90
R / Rfree (%) 15.6 / 18.2

Other elements in 7uld:

The structure of Gtp 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 Gtp Complex of F420-Gamma Glutamyl Ligase (Cofe) From Archaeoglobus Fulgidus (pdb code 7uld). 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 Gtp Complex of F420-Gamma Glutamyl Ligase (Cofe) From Archaeoglobus Fulgidus, PDB code: 7uld:

Sodium binding site 1 out of 1 in 7uld

Go back to Sodium Binding Sites List in 7uld
Sodium binding site 1 out of 1 in the Gtp 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 Gtp Complex of F420-Gamma Glutamyl Ligase (Cofe) From Archaeoglobus Fulgidus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na304

b:32.2
occ:1.00
 OD2 A:ASP150 2.3 28.3 1.0
ND2 A:ASN101 2.9 15.7 1.0
ND2 A:ASN152 3.0 15.5 1.0
CG A:ASP150 3.4 19.3 1.0
SG A:CYS103 3.5 17.3 1.0
CB A:CYS103 3.7 15.7 1.0
CZ A:PHE99 3.7 20.9 1.0
CB A:ASP150 3.8 14.8 1.0
CG A:ASN152 3.8 13.5 1.0
OD1 A:ASN152 3.9 17.2 1.0
O A:HOH476 3.9 34.5 1.0
CA A:GLY107 4.0 16.7 1.0
CG A:ASN101 4.1 16.0 1.0
O A:HOH547 4.2 30.5 1.0
O A:HOH418 4.3 34.4 1.0
CG2 A:ILE165 4.3 12.8 1.0
CB A:ASN101 4.4 16.4 1.0
OD1 A:ASP150 4.4 18.9 1.0
CE2 A:PHE99 4.5 22.3 1.0
N A:GLY107 4.5 15.0 1.0
CE1 A:PHE99 4.6 22.4 1.0
O A:THR151 5.0 12.9 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 09:14:47 2024

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