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Fluorine in PDB 1e73: 2-F-Glucosylated Myrosinase From Sinapis Alba with Bound L-Ascorbate

Enzymatic activity of 2-F-Glucosylated Myrosinase From Sinapis Alba with Bound L-Ascorbate

All present enzymatic activity of 2-F-Glucosylated Myrosinase From Sinapis Alba with Bound L-Ascorbate:
3.2.1.147;

Protein crystallography data

The structure of 2-F-Glucosylated Myrosinase From Sinapis Alba with Bound L-Ascorbate, PDB code: 1e73 was solved by W.P.Burmeister, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.50
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 135.300, 137.200, 80.600, 90.00, 90.00, 90.00
R / Rfree (%) 13.4 / 16.7

Other elements in 1e73:

The structure of 2-F-Glucosylated Myrosinase From Sinapis Alba with Bound L-Ascorbate also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the 2-F-Glucosylated Myrosinase From Sinapis Alba with Bound L-Ascorbate (pdb code 1e73). 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 2-F-Glucosylated Myrosinase From Sinapis Alba with Bound L-Ascorbate, PDB code: 1e73:

Fluorine binding site 1 out of 1 in 1e73

Go back to Fluorine Binding Sites List in 1e73
Fluorine binding site 1 out of 1 in the 2-F-Glucosylated Myrosinase From Sinapis Alba with Bound L-Ascorbate


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of 2-F-Glucosylated Myrosinase From Sinapis Alba with Bound L-Ascorbate within 5.0Å range:
probe atom residue distance (Å) B Occ
M:F999

b:22.1
occ:1.00
 F2 M:G2F999 0.0 22.1 1.0
C2 M:G2F999 1.4 26.3 1.0
C1 M:G2F999 2.3 27.2 1.0
C3 M:G2F999 2.4 26.3 1.0
OE2 M:GLU409 2.7 21.7 1.0
O3 M:G2F999 2.8 18.7 1.0
ND2 M:ASN186 2.9 11.6 1.0
OE1 M:GLU409 3.0 20.2 1.0
NE2 M:HIS141 3.1 11.3 1.0
CD M:GLU409 3.3 23.8 1.0
CE1 M:HIS141 3.3 12.8 1.0
O5 M:G2F999 3.5 28.2 1.0
OE1 M:GLN187 3.7 11.2 1.0
C4 M:G2F999 3.7 28.1 1.0
OD1 M:ASN186 3.7 12.4 1.0
CG M:ASN186 3.7 11.6 1.0
O M:HOH2757 4.0 27.0 1.0
CD M:GLN187 4.0 10.8 1.0
C5 M:G2F999 4.1 30.9 1.0
CD2 M:HIS141 4.2 11.6 1.0
ND2 M:ASN328 4.3 10.7 1.0
O M:HOH2348 4.3 67.4 1.0
CG M:GLN187 4.5 10.6 1.0
ND1 M:HIS141 4.5 11.7 1.0
NE2 M:GLN187 4.5 11.0 1.0
CH2 M:TRP142 4.6 14.5 1.0
CZ2 M:TRP142 4.6 12.7 1.0
CG M:GLU409 4.7 20.6 1.0
O4 M:G2F999 4.8 24.1 1.0
CZ3 M:TRP457 5.0 13.2 1.0

Reference:

W.P.Burmeister, S.Cottaz, P.Rollin, A.Vasella, B.Henrissat. High Resolution X-Ray Crystallography Shows That Ascorbate Is A Cofactor For Myrosinase and Substitutes For the Function of the Catalytic Base J.Biol.Chem. V. 275 39385 2000.
ISSN: ISSN 0021-9258
PubMed: 10978344
DOI: 10.1074/JBC.M006796200
Page generated: Wed Jul 31 11:09:32 2024

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