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Fluorine in PDB 3f9m: Human Pancreatic Glucokinase in Complex with Glucose and Activator Showing A Mobile Flap

Enzymatic activity of Human Pancreatic Glucokinase in Complex with Glucose and Activator Showing A Mobile Flap

All present enzymatic activity of Human Pancreatic Glucokinase in Complex with Glucose and Activator Showing A Mobile Flap:
2.7.1.2;

Protein crystallography data

The structure of Human Pancreatic Glucokinase in Complex with Glucose and Activator Showing A Mobile Flap, PDB code: 3f9m was solved by P.Petit, L.Gluais, A.Lagarde, L.Vuillard, J.A.Boutin, G.Ferry, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.74 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 65.700, 81.200, 85.600, 90.00, 90.00, 90.00
R / Rfree (%) 19 / 22.2

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Human Pancreatic Glucokinase in Complex with Glucose and Activator Showing A Mobile Flap (pdb code 3f9m). 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 Human Pancreatic Glucokinase in Complex with Glucose and Activator Showing A Mobile Flap, PDB code: 3f9m:

Fluorine binding site 1 out of 1 in 3f9m

Go back to Fluorine Binding Sites List in 3f9m
Fluorine binding site 1 out of 1 in the Human Pancreatic Glucokinase in Complex with Glucose and Activator Showing A Mobile Flap


Mono view


Stereo pair view

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

b:25.5
occ:1.00
 F14 A:MRK501 0.0 25.5 1.0
C13 A:MRK501 1.4 23.6 1.0
C15 A:MRK501 2.4 22.4 1.0
C12 A:MRK501 2.4 23.8 1.0
C18 A:MRK501 3.0 27.1 1.0
S16 A:MRK501 3.0 26.2 1.0
N17 A:MRK501 3.1 28.1 1.0
CG A:TYR214 3.2 23.9 1.0
CD2 A:TYR214 3.4 23.2 1.0
C22 A:MRK501 3.4 24.9 1.0
CD1 A:ILE211 3.5 19.0 1.0
CB A:TYR214 3.6 23.6 1.0
CD1 A:TYR214 3.6 24.2 1.0
C9 A:MRK501 3.6 23.2 1.0
C11 A:MRK501 3.6 23.1 1.0
N19 A:MRK501 3.7 28.6 1.0
C21 A:MRK501 3.9 27.7 1.0
CE2 A:TYR214 3.9 24.3 1.0
O A:THR65 3.9 31.9 1.0
CE1 A:TYR214 4.1 23.6 1.0
C10 A:MRK501 4.1 22.3 1.0
C20 A:MRK501 4.2 29.5 1.0
CZ A:TYR214 4.2 23.9 1.0
CG2 A:ILE211 4.7 13.2 1.0
N23 A:MRK501 4.7 23.0 1.0
CA A:ILE211 4.7 13.1 1.0
CG1 A:ILE211 4.8 15.4 1.0
OH A:TYR215 5.0 27.9 1.0
CB A:ILE211 5.0 14.0 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: Sun Dec 13 11:45:51 2020

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