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Fluorine in PDB 1iew: Crystal Structure of Barley Beta-D-Glucan Glucohydrolase Isoenzyme EXO1 in Complex with 2-Deoxy-2-Fluoro-Alpha-D-Glucoside

Enzymatic activity of Crystal Structure of Barley Beta-D-Glucan Glucohydrolase Isoenzyme EXO1 in Complex with 2-Deoxy-2-Fluoro-Alpha-D-Glucoside

All present enzymatic activity of Crystal Structure of Barley Beta-D-Glucan Glucohydrolase Isoenzyme EXO1 in Complex with 2-Deoxy-2-Fluoro-Alpha-D-Glucoside:
3.2.1.58;

Protein crystallography data

The structure of Crystal Structure of Barley Beta-D-Glucan Glucohydrolase Isoenzyme EXO1 in Complex with 2-Deoxy-2-Fluoro-Alpha-D-Glucoside, PDB code: 1iew was solved by M.Hrmova, R.Degori, G.B.Fincher, B.J.Smith, J.N.Varghese, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.55
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 100.962, 100.962, 181.254, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 23.3

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Barley Beta-D-Glucan Glucohydrolase Isoenzyme EXO1 in Complex with 2-Deoxy-2-Fluoro-Alpha-D-Glucoside (pdb code 1iew). 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 Crystal Structure of Barley Beta-D-Glucan Glucohydrolase Isoenzyme EXO1 in Complex with 2-Deoxy-2-Fluoro-Alpha-D-Glucoside, PDB code: 1iew:

Fluorine binding site 1 out of 1 in 1iew

Go back to Fluorine Binding Sites List in 1iew
Fluorine binding site 1 out of 1 in the Crystal Structure of Barley Beta-D-Glucan Glucohydrolase Isoenzyme EXO1 in Complex with 2-Deoxy-2-Fluoro-Alpha-D-Glucoside


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Barley Beta-D-Glucan Glucohydrolase Isoenzyme EXO1 in Complex with 2-Deoxy-2-Fluoro-Alpha-D-Glucoside within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F620

b:29.1
occ:1.00
 F2 A:G2F620 0.0 29.1 1.0
C2 A:G2F620 1.4 29.5 1.0
C1 A:G2F620 2.4 28.7 1.0
C3 A:G2F620 2.4 28.7 1.0
OD2 A:ASP285 2.6 32.7 1.0
O3 A:G2F620 2.8 29.0 1.0
NH1 A:ARG158 2.9 18.2 1.0
OD1 A:ASP285 2.9 28.2 1.0
CG A:ASP285 3.1 28.2 1.0
CE2 A:TYR253 3.3 39.4 1.0
O5 A:G2F620 3.7 28.4 1.0
C4 A:G2F620 3.7 29.0 1.0
NE2 A:HIS207 3.9 21.4 1.0
CZ A:ARG158 3.9 21.2 1.0
OE1 A:GLU491 4.0 28.5 1.0
CD2 A:TYR253 4.0 36.4 1.0
O A:HOH926 4.1 22.5 1.0
CZ A:TYR253 4.1 40.5 1.0
NH2 A:ARG158 4.1 20.3 1.0
OH A:TYR253 4.2 41.9 1.0
C5 A:G2F620 4.2 28.6 1.0
CD A:GLU491 4.2 27.0 1.0
O A:HOH732 4.2 33.0 1.0
CD2 A:HIS207 4.3 22.7 1.0
OE2 A:GLU491 4.4 23.9 1.0
CB A:ASP285 4.5 25.0 1.0
CE1 A:HIS207 4.6 20.4 1.0
O A:HOH929 4.8 17.4 1.0
O4 A:G2F620 4.9 29.9 1.0
CG A:GLU491 5.0 25.5 1.0

Reference:

M.Hrmova, J.N.Varghese, R.De Gori, B.J.Smith, H.Driguez, G.B.Fincher. Catalytic Mechanisms and Reaction Intermediates Along the Hydrolytic Pathway of A Plant Beta-D-Glucan Glucohydrolase. Structure V. 9 1005 2001.
ISSN: ISSN 0969-2126
PubMed: 11709165
DOI: 10.1016/S0969-2126(01)00673-6
Page generated: Mon Jul 14 10:58:03 2025

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