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Fluorine in PDB 3id8: Ternary Complex of Human Pancreatic Glucokinase Crystallized with Activator, Glucose and Amp-Pnp

Enzymatic activity of Ternary Complex of Human Pancreatic Glucokinase Crystallized with Activator, Glucose and Amp-Pnp

All present enzymatic activity of Ternary Complex of Human Pancreatic Glucokinase Crystallized with Activator, Glucose and Amp-Pnp:
2.7.1.2;

Protein crystallography data

The structure of Ternary Complex of Human Pancreatic Glucokinase Crystallized with Activator, Glucose and Amp-Pnp, PDB code: 3id8 was solved by P.Petit, L.Gluais, 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) 19.94 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 67.000, 82.600, 86.800, 90.00, 90.00, 90.00
R / Rfree (%) 20.1 / 27.9

Other elements in 3id8:

The structure of Ternary Complex of Human Pancreatic Glucokinase Crystallized with Activator, Glucose and Amp-Pnp also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Potassium (K) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Ternary Complex of Human Pancreatic Glucokinase Crystallized with Activator, Glucose and Amp-Pnp (pdb code 3id8). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Ternary Complex of Human Pancreatic Glucokinase Crystallized with Activator, Glucose and Amp-Pnp, PDB code: 3id8:

Fluorine binding site 1 out of 1 in 3id8

Go back to Fluorine Binding Sites List in 3id8
Fluorine binding site 1 out of 1 in the Ternary Complex of Human Pancreatic Glucokinase Crystallized with Activator, Glucose and Amp-Pnp


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Ternary Complex of Human Pancreatic Glucokinase Crystallized with Activator, Glucose and Amp-Pnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F501

b:38.2
occ:1.00
 F14 A:MRK501 0.0 38.2 1.0
C13 A:MRK501 1.4 38.1 1.0
C15 A:MRK501 2.4 35.9 1.0
C12 A:MRK501 2.4 38.3 1.0
C18 A:MRK501 3.0 37.6 1.0
S16 A:MRK501 3.1 39.6 1.0
N17 A:MRK501 3.2 37.6 1.0
CD2 A:TYR214 3.3 39.2 1.0
CG A:TYR214 3.3 38.3 1.0
C22 A:MRK501 3.5 36.8 1.0
CE2 A:TYR214 3.6 39.5 1.0
C9 A:MRK501 3.6 35.8 1.0
N19 A:MRK501 3.7 38.0 1.0
CD1 A:TYR214 3.7 38.3 1.0
C11 A:MRK501 3.7 37.3 1.0
CB A:TYR214 3.9 38.1 1.0
CZ A:TYR214 3.9 39.9 1.0
CE1 A:TYR214 4.0 39.1 1.0
C21 A:MRK501 4.0 36.7 1.0
CD1 A:ILE211 4.1 23.8 1.0
C20 A:MRK501 4.1 37.6 1.0
C10 A:MRK501 4.2 35.2 1.0
N23 A:MRK501 4.7 35.7 1.0
O A:SER64 4.8 47.9 1.0
OH A:TYR214 4.8 39.5 1.0
OH A:TYR215 4.9 43.7 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 Jul 31 19:29:04 2024

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