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Fluorine in PDB 2c1z: Structure and Activity of A Flavonoid 3-O Glucosyltransferase Reveals the Basis For Plant Natural Product Modification

Enzymatic activity of Structure and Activity of A Flavonoid 3-O Glucosyltransferase Reveals the Basis For Plant Natural Product Modification

All present enzymatic activity of Structure and Activity of A Flavonoid 3-O Glucosyltransferase Reveals the Basis For Plant Natural Product Modification:
2.4.1.91;

Protein crystallography data

The structure of Structure and Activity of A Flavonoid 3-O Glucosyltransferase Reveals the Basis For Plant Natural Product Modification, PDB code: 2c1z was solved by W.Offen, C.Martinez-Fleites, E.Kiat-Lim, M.Yang, B.G.Davis, C.A.Tarling, C.M.Ford, D.J.Bowles, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.78 / 1.9
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.106, 93.531, 106.670, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 23.2

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Structure and Activity of A Flavonoid 3-O Glucosyltransferase Reveals the Basis For Plant Natural Product Modification (pdb code 2c1z). 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 Structure and Activity of A Flavonoid 3-O Glucosyltransferase Reveals the Basis For Plant Natural Product Modification, PDB code: 2c1z:

Fluorine binding site 1 out of 1 in 2c1z

Go back to Fluorine Binding Sites List in 2c1z
Fluorine binding site 1 out of 1 in the Structure and Activity of A Flavonoid 3-O Glucosyltransferase Reveals the Basis For Plant Natural Product Modification


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure and Activity of A Flavonoid 3-O Glucosyltransferase Reveals the Basis For Plant Natural Product Modification within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F1457

b:30.6
occ:1.00
 F1 A:U2F1457 0.0 30.6 1.0
C2 A:U2F1457 1.4 29.5 1.0
C1 A:U2F1457 2.4 29.8 1.0
C3 A:U2F1457 2.4 27.0 1.0
O2B A:U2F1457 2.8 30.8 1.0
O1 A:U2F1457 2.8 29.3 1.0
O3 A:U2F1457 2.8 28.8 1.0
NE2 A:GLN375 3.0 19.0 1.0
CZ A:PHE372 3.3 24.9 1.0
PB A:U2F1457 3.4 30.9 1.0
O5 A:U2F1457 3.6 31.6 1.0
CE1 A:PHE372 3.6 27.7 1.0
C4 A:U2F1457 3.8 26.7 1.0
NE2 A:HIS350 3.9 24.9 1.0
CD2 A:HIS350 4.1 23.8 1.0
C5 A:U2F1457 4.1 27.8 1.0
O A:HOH2200 4.2 39.9 1.0
CE2 A:PHE372 4.2 27.2 1.0
CD A:GLN375 4.2 20.3 1.0
O3A A:U2F1457 4.3 26.9 1.0
CG2 A:VAL281 4.5 42.0 1.0
O1B A:U2F1457 4.5 28.8 1.0
CD1 A:PHE372 4.8 27.6 1.0
O4 A:U2F1457 4.8 20.2 1.0
CG A:GLN375 4.8 17.2 1.0
C9 A:KMP1456 5.0 34.5 1.0
C10 A:KMP1456 5.0 34.0 1.0

Reference:

W.Offen, C.Martinez-Fleites, M.Yang, E.Kiat-Lim, B.G.Davis, C.A.Tarling, C.M.Ford, D.J.Bowles, G.J.Davies. Structure of A Flavonoid Glucosyltransferase Reveals the Basis For Plant Natural Product Modification. Embo J. V. 25 1396 2006.
ISSN: ISSN 0261-4189
PubMed: 16482224
DOI: 10.1038/SJ.EMBOJ.7600970
Page generated: Mon Jul 14 12:44:54 2025

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