Manganese 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:

Sodium (Na) 1 atom

Manganese Binding Sites:

The binding sites of Manganese 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 Manganese atom.
In total 2 binding sites of Manganese where determined in the Gtp Complex of F420-Gamma Glutamyl Ligase (Cofe) From Archaeoglobus Fulgidus, PDB code: 7uld:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 7uld

Go back to Manganese Binding Sites List in 7uld
Manganese binding site 1 out of 2 in the Gtp Complex of F420-Gamma Glutamyl Ligase (Cofe) From Archaeoglobus Fulgidus


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn 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:Mn302

b:13.8
occ:1.00
O3G A:GTP305 2.1 14.7 1.0
O2B A:GTP305 2.1 13.4 1.0
OE1 A:GLU208 2.2 14.3 1.0
O A:HOH407 2.2 13.9 1.0
O1A A:GTP305 2.2 12.6 1.0
OG1 A:THR151 2.3 14.9 1.0
CD A:GLU208 3.0 14.3 1.0
PB A:GTP305 3.2 13.3 1.0
CB A:THR151 3.2 13.2 1.0
PG A:GTP305 3.3 15.0 1.0
OE2 A:GLU208 3.3 16.3 1.0
O3B A:GTP305 3.4 14.0 1.0
PA A:GTP305 3.5 12.4 1.0
O3A A:GTP305 3.6 13.4 1.0
O A:HOH474 3.9 18.6 1.0
O A:HOH468 4.0 14.7 1.0
OD1 A:ASN203 4.1 13.6 1.0
CG2 A:THR151 4.1 15.1 1.0
O2G A:GTP305 4.1 19.3 1.0
O A:GLY207 4.3 14.3 1.0
CG A:GLU208 4.4 14.5 1.0
CA A:GLU208 4.4 13.9 1.0
N A:THR151 4.4 10.6 1.0
CA A:THR151 4.4 10.7 1.0
O1G A:GTP305 4.4 17.7 1.0
O5' A:GTP305 4.5 12.7 1.0
C5' A:GTP305 4.5 11.1 1.0
O2A A:GTP305 4.5 13.5 1.0
O1B A:GTP305 4.5 13.5 1.0
CB A:GLU208 4.7 14.4 1.0
CG A:ASN203 5.0 11.3 1.0

Manganese binding site 2 out of 2 in 7uld

Go back to Manganese Binding Sites List in 7uld
Manganese binding site 2 out of 2 in the Gtp Complex of F420-Gamma Glutamyl Ligase (Cofe) From Archaeoglobus Fulgidus


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Gtp Complex of F420-Gamma Glutamyl Ligase (Cofe) From Archaeoglobus Fulgidus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn303

b:22.7
occ:1.00
O2G A:GTP305 2.0 19.3 1.0
OD1 A:ASP150 2.1 18.9 1.0
OD2 A:ASP109 2.1 23.1 1.0
O A:HOH442 2.1 17.6 1.0
O A:HOH547 2.3 30.5 1.0
O A:HOH418 2.4 34.4 1.0
CG A:ASP150 2.9 19.3 1.0
CG A:ASP109 3.0 18.5 1.0
OD2 A:ASP150 3.1 28.3 1.0
PG A:GTP305 3.3 15.0 1.0
OD1 A:ASP109 3.3 19.6 1.0
O3B A:GTP305 3.6 14.0 1.0
O1G A:GTP305 3.8 17.7 1.0
O A:GLY107 3.8 17.3 1.0
O A:HOH489 4.0 19.5 1.0
OG A:SER40 4.1 19.4 1.0
O1B A:GTP305 4.3 13.5 1.0
CB A:ASP150 4.3 14.8 1.0
CB A:ASP109 4.4 16.3 1.0
PB A:GTP305 4.4 13.3 1.0
O A:HOH507 4.5 16.0 1.0
C A:GLY107 4.5 16.0 1.0
O3G A:GTP305 4.5 14.7 1.0
CA A:GLY107 4.6 16.7 1.0
N A:THR151 4.7 10.6 1.0
O A:THR151 4.7 12.9 1.0
O A:HOH401 4.7 29.4 1.0
CA A:ASP150 4.8 11.4 1.0
OG1 A:THR41 4.9 14.1 1.0
O2B A:GTP305 4.9 13.4 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: Tue Apr 25 23:47:58 2023

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