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Magnesium in PDB 3fgu: Catalytic Complex of Human Glucokinase

Enzymatic activity of Catalytic Complex of Human Glucokinase

All present enzymatic activity of Catalytic Complex of Human Glucokinase:
2.7.1.2;

Protein crystallography data

The structure of Catalytic Complex of Human Glucokinase, PDB code: 3fgu was solved by P.Petit, A.Lagarde, J.A.Boutin, G.Ferry, L.Vuillard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.15
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 65.880, 82.120, 86.830, 90.00, 90.00, 90.00
R / Rfree (%) 19.7 / 25.5

Other elements in 3fgu:

The structure of Catalytic Complex of Human Glucokinase also contains other interesting chemical elements:

Potassium (K) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Catalytic Complex of Human Glucokinase (pdb code 3fgu). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Catalytic Complex of Human Glucokinase, PDB code: 3fgu:

Magnesium binding site 1 out of 1 in 3fgu

Go back to Magnesium Binding Sites List in 3fgu
Magnesium binding site 1 out of 1 in the Catalytic Complex of Human Glucokinase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Catalytic Complex of Human Glucokinase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg700

b:40.8
occ:1.00
OD1 A:ASP205 2.7 12.6 1.0
O A:HOH550 2.7 26.9 1.0
O A:HOH560 3.0 30.8 1.0
O2B A:ANP600 3.2 28.4 0.5
O3G A:ANP600 3.2 20.0 0.5
CB A:ASP205 3.4 15.1 1.0
CG A:ASP205 3.5 13.7 1.0
O1B A:ANP600 3.6 27.5 0.5
O2G A:ANP600 3.8 20.0 0.5
PB A:ANP600 3.8 31.0 0.5
PG A:ANP600 4.0 20.0 0.5
OG A:SER151 4.1 19.1 1.0
O6 A:BGC501 4.2 12.8 1.0
O A:HOH642 4.3 40.9 1.0
CD1 A:ILE225 4.4 6.1 1.0
N3B A:ANP600 4.5 30.7 0.5
OD2 A:ASP78 4.5 22.0 1.0
CG2 A:ILE225 4.5 8.9 1.0
OD2 A:ASP205 4.7 16.0 1.0
OD1 A:ASP78 4.7 24.1 1.0
CB A:SER151 4.8 16.5 1.0
CA A:ASP205 4.9 14.9 1.0
CG1 A:ILE225 4.9 11.2 1.0

Reference:

P.Petit, M.Antoine, G.Ferry, J.A.Boutin, A.Lagarde, L.Gluais, R.Vincentelli, L.Vuillard. The Active Conformation of Human Glucokinase Is Not Altered By Allosteric Activators Acta Crystallogr.,Sect.D V. 67 929 2011.
ISSN: ISSN 0907-4449
PubMed: 22101819
DOI: 10.1107/S0907444911036729
Page generated: Wed Aug 14 13:46:38 2024

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