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Manganese 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:

Sodium (Na) 1 atom

Manganese Binding Sites:

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

Manganese binding site 1 out of 2 in 7ule

Go back to Manganese Binding Sites List in 7ule
Manganese binding site 1 out of 2 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 Manganese with other atoms in the Mn 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:Mn303

b:29.4
occ:1.00
O A:HOH444 2.0 29.0 1.0
O1B A:GDP301 2.0 33.9 1.0
O A:HOH405 2.0 31.2 1.0
O1A A:GDP301 2.0 33.2 1.0
OE1 A:GLU208 2.0 32.7 1.0
OG1 A:THR151 2.0 28.4 1.0
CD A:GLU208 2.9 34.2 1.0
PB A:GDP301 3.1 32.3 1.0
CB A:THR151 3.1 28.2 1.0
PA A:GDP301 3.3 35.4 1.0
OE2 A:GLU208 3.3 34.8 1.0
O3A A:GDP301 3.5 33.5 1.0
O2B A:GDP301 3.6 32.4 1.0
O A:HOH437 3.9 38.2 1.0
CG2 A:THR151 4.0 28.4 1.0
OD1 A:ASN203 4.1 29.5 1.0
O A:HOH474 4.1 26.9 1.0
O A:HOH490 4.1 35.9 1.0
N A:THR151 4.2 26.5 1.0
CG A:GLU208 4.2 34.0 1.0
CA A:THR151 4.2 26.8 1.0
O5' A:GDP301 4.3 33.5 1.0
C5' A:GDP301 4.3 33.9 1.0
O A:GLY207 4.4 32.3 1.0
CA A:GLU208 4.4 34.1 1.0
O2A A:GDP301 4.4 33.3 1.0
O3B A:GDP301 4.5 32.2 1.0
CB A:GLU208 4.6 33.9 1.0
O3I A:F4I302 4.6 35.6 1.0
CG A:ASN203 5.0 29.5 1.0

Manganese binding site 2 out of 2 in 7ule

Go back to Manganese Binding Sites List in 7ule
Manganese binding site 2 out of 2 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 Manganese with other atoms in the Mn binding site number 2 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:Mn304

b:33.0
occ:1.00
O A:HOH401 2.0 34.8 1.0
O A:HOH449 2.0 35.5 1.0
O2B A:GDP301 2.0 32.4 1.0
O A:HOH446 2.0 38.1 1.0
OD2 A:ASP109 2.0 36.3 1.0
OD1 A:ASP150 2.0 30.9 1.0
CG A:ASP109 3.0 35.8 1.0
CG A:ASP150 3.0 27.6 1.0
PB A:GDP301 3.3 32.3 1.0
OD2 A:ASP150 3.4 29.5 1.0
OD1 A:ASP109 3.5 36.2 1.0
O3B A:GDP301 3.7 32.2 1.0
NA A:NA305 3.7 37.3 1.0
O A:HOH405 3.8 31.2 1.0
OG A:SER40 4.0 31.5 1.0
O1B A:GDP301 4.1 33.9 1.0
CB A:ASP109 4.2 35.2 1.0
O A:HOH458 4.3 34.5 1.0
OG1 A:THR41 4.3 34.1 1.0
CB A:ASP150 4.4 28.0 1.0
O A:HOH453 4.4 36.0 1.0
N A:THR151 4.5 26.5 1.0
O A:GLY107 4.5 32.2 1.0
O A:THR151 4.5 26.4 1.0
O3A A:GDP301 4.5 33.5 1.0
O3I A:F4I302 4.6 35.6 1.0
CA A:ASP150 4.8 26.4 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: Sun Oct 6 10:54:45 2024

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