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Fluorine in PDB 1uys: Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop

Enzymatic activity of Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop

All present enzymatic activity of Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop:
6.4.1.2;

Protein crystallography data

The structure of Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop, PDB code: 1uys was solved by H.Zhang, B.Tweel, L.Tong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.42 / 2.8
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 246.210, 125.580, 146.880, 90.00, 94.08, 90.00
R / Rfree (%) 21.8 / 25.2

Other elements in 1uys:

The structure of Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop also contains other interesting chemical elements:

Chlorine (Cl) 3 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop (pdb code 1uys). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 9 binding sites of Fluorine where determined in the Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop, PDB code: 1uys:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9;

Fluorine binding site 1 out of 9 in 1uys

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Fluorine binding site 1 out of 9 in the Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F3000

b:46.9
occ:1.00
 F1 A:H1L3000 0.0 46.9 1.0
C12 A:H1L3000 1.3 44.5 1.0
F3 A:H1L3000 2.2 45.4 1.0
F2 A:H1L3000 2.2 44.5 1.0
C11 A:H1L3000 2.3 42.9 1.0
C10 A:H1L3000 2.7 42.1 1.0
C13 A:H1L3000 3.6 43.3 1.0
N9 A:H1L3000 4.0 40.5 1.0
C14 A:H1L3000 4.7 43.7 1.0
C9 A:H1L3000 4.9 40.6 1.0

Fluorine binding site 2 out of 9 in 1uys

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Fluorine binding site 2 out of 9 in the Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F3000

b:44.5
occ:1.00
 F2 A:H1L3000 0.0 44.5 1.0
C12 A:H1L3000 1.3 44.5 1.0
F3 A:H1L3000 2.2 45.4 1.0
F1 A:H1L3000 2.2 46.9 1.0
C11 A:H1L3000 2.3 42.9 1.0
C13 A:H1L3000 2.9 43.3 1.0
C10 A:H1L3000 3.4 42.1 1.0
C14 A:H1L3000 4.2 43.7 1.0
N9 A:H1L3000 4.5 40.5 1.0
C9 A:H1L3000 4.8 40.6 1.0

Fluorine binding site 3 out of 9 in 1uys

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Fluorine binding site 3 out of 9 in the Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F3000

b:45.4
occ:1.00
 F3 A:H1L3000 0.0 45.4 1.0
C12 A:H1L3000 1.3 44.5 1.0
F1 A:H1L3000 2.2 46.9 1.0
F2 A:H1L3000 2.2 44.5 1.0
C11 A:H1L3000 2.3 42.9 1.0
C13 A:H1L3000 2.9 43.3 1.0
C10 A:H1L3000 3.4 42.1 1.0
C14 A:H1L3000 4.2 43.7 1.0
N9 A:H1L3000 4.6 40.5 1.0
C9 A:H1L3000 4.9 40.6 1.0

Fluorine binding site 4 out of 9 in 1uys

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Fluorine binding site 4 out of 9 in the Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F3000

b:57.6
occ:1.00
 F1 B:H1L3000 0.0 57.6 1.0
C12 B:H1L3000 1.3 56.6 1.0
F3 B:H1L3000 2.2 54.9 1.0
F2 B:H1L3000 2.2 54.7 1.0
C11 B:H1L3000 2.4 57.0 1.0
C10 B:H1L3000 2.9 56.7 1.0
CE3 C:TRP1924 3.0 39.0 1.0
CZ3 C:TRP1924 3.1 40.7 1.0
CG2 C:VAL2002 3.3 23.9 1.0
CD2 C:TRP1924 3.3 39.6 1.0
CG1 C:VAL2002 3.4 21.4 1.0
CH2 C:TRP1924 3.5 40.3 1.0
C13 B:H1L3000 3.6 59.2 1.0
CE2 C:TRP1924 3.6 38.7 1.0
CZ2 C:TRP1924 3.8 37.6 1.0
CB C:VAL2002 3.8 20.9 1.0
CG C:TRP1924 4.1 41.4 1.0
CD1 C:ILE1974 4.1 21.7 1.0
N9 B:H1L3000 4.2 57.1 1.0
O C:GLY1998 4.4 32.5 1.0
NE1 C:TRP1924 4.5 39.9 1.0
CB C:TRP1924 4.7 41.6 1.0
CA C:SER1999 4.7 27.5 1.0
CD1 C:TRP1924 4.7 41.6 1.0
C14 B:H1L3000 4.7 60.1 1.0
C9 B:H1L3000 4.9 57.2 1.0
C C:GLY1998 5.0 29.9 1.0

Fluorine binding site 5 out of 9 in 1uys

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Fluorine binding site 5 out of 9 in the Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F3000

b:54.7
occ:1.00
 F2 B:H1L3000 0.0 54.7 1.0
C12 B:H1L3000 1.3 56.6 1.0
F3 B:H1L3000 2.2 54.9 1.0
F1 B:H1L3000 2.2 57.6 1.0
C11 B:H1L3000 2.3 57.0 1.0
C13 B:H1L3000 2.7 59.2 1.0
CD1 C:ILE1974 3.5 21.7 1.0
CA C:GLY1971 3.6 34.5 1.0
C10 B:H1L3000 3.6 56.7 1.0
CB C:ALA1929 4.0 20.0 1.0
C14 B:H1L3000 4.1 60.1 1.0
CG1 C:VAL2002 4.2 21.4 1.0
N C:GLY1971 4.4 35.5 1.0
O C:VAL1967 4.4 40.1 1.0
CD2 C:TRP1924 4.4 39.6 1.0
CG1 C:VAL1967 4.5 41.1 1.0
CE2 C:TRP1924 4.5 38.7 1.0
CG1 C:ILE1974 4.6 20.6 1.0
CG C:TRP1924 4.6 41.4 1.0
CE3 C:TRP1924 4.7 39.0 1.0
N9 B:H1L3000 4.7 57.1 1.0
C C:GLY1971 4.7 32.6 1.0
O C:GLY1971 4.7 33.0 1.0
NE1 C:TRP1924 4.8 39.9 1.0
CA C:ALA1929 4.8 22.2 1.0
CD1 C:TRP1924 4.9 41.6 1.0
O C:TYR1970 4.9 36.9 1.0
C9 B:H1L3000 4.9 57.2 1.0
CB C:VAL2002 4.9 20.9 1.0
CZ2 C:TRP1924 4.9 37.6 1.0
C C:TYR1970 4.9 36.3 1.0
CG2 C:VAL2002 5.0 23.9 1.0

Fluorine binding site 6 out of 9 in 1uys

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Fluorine binding site 6 out of 9 in the Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F3000

b:54.9
occ:1.00
 F3 B:H1L3000 0.0 54.9 1.0
C12 B:H1L3000 1.3 56.6 1.0
F2 B:H1L3000 2.2 54.7 1.0
F1 B:H1L3000 2.2 57.6 1.0
C11 B:H1L3000 2.3 57.0 1.0
CG C:TRP1924 3.1 41.4 1.0
C10 B:H1L3000 3.1 56.7 1.0
CD2 C:TRP1924 3.1 39.6 1.0
C13 B:H1L3000 3.2 59.2 1.0
CB C:TRP1924 3.2 41.6 1.0
CE3 C:TRP1924 3.4 39.0 1.0
CD1 C:TRP1924 3.8 41.6 1.0
CG1 C:VAL1967 3.8 41.1 1.0
CE2 C:TRP1924 3.9 38.7 1.0
CZ3 C:TRP1924 4.2 40.7 1.0
NE1 C:TRP1924 4.2 39.9 1.0
N9 B:H1L3000 4.3 57.1 1.0
CB C:PHE1956 4.4 51.6 1.0
C14 B:H1L3000 4.4 60.1 1.0
CD2 C:PHE1956 4.4 50.2 1.0
CB C:ALA1929 4.5 20.0 1.0
CZ2 C:TRP1924 4.7 37.6 1.0
CA C:TRP1924 4.7 43.2 1.0
CG C:PHE1956 4.7 51.0 1.0
CH2 C:TRP1924 4.8 40.3 1.0
C9 B:H1L3000 4.8 57.2 1.0

Fluorine binding site 7 out of 9 in 1uys

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Fluorine binding site 7 out of 9 in the Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 7 of Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop within 5.0Å range:
probe atom residue distance (Å) B Occ
C:F3000

b:56.3
occ:1.00
 F1 C:H1L3000 0.0 56.3 1.0
C12 C:H1L3000 1.3 55.3 1.0
F3 C:H1L3000 2.2 54.0 1.0
F2 C:H1L3000 2.2 52.8 1.0
C11 C:H1L3000 2.3 56.9 1.0
C10 C:H1L3000 2.9 58.5 1.0
CG1 B:VAL2002 3.2 22.6 1.0
CG2 B:VAL2002 3.3 23.7 1.0
CE3 B:TRP1924 3.4 46.3 1.0
C13 C:H1L3000 3.5 60.7 1.0
CZ3 B:TRP1924 3.6 49.3 1.0
CD2 B:TRP1924 3.6 46.1 1.0
CB B:VAL2002 3.7 22.3 1.0
CH2 B:TRP1924 3.9 47.4 1.0
CE2 B:TRP1924 4.0 46.3 1.0
CD1 B:ILE1974 4.0 17.2 1.0
CZ2 B:TRP1924 4.1 46.6 1.0
N9 C:H1L3000 4.2 59.5 1.0
CG B:TRP1924 4.3 47.7 1.0
O B:GLY1998 4.6 30.5 1.0
C14 C:H1L3000 4.6 61.9 1.0
NE1 B:TRP1924 4.7 46.2 1.0
CB B:TRP1924 4.8 46.3 1.0
CD1 B:TRP1924 4.8 48.2 1.0
C9 C:H1L3000 4.9 60.3 1.0
CA B:SER1999 5.0 27.8 1.0

Fluorine binding site 8 out of 9 in 1uys

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Fluorine binding site 8 out of 9 in the Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 8 of Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop within 5.0Å range:
probe atom residue distance (Å) B Occ
C:F3000

b:52.8
occ:1.00
 F2 C:H1L3000 0.0 52.8 1.0
C12 C:H1L3000 1.3 55.3 1.0
F3 C:H1L3000 2.2 54.0 1.0
F1 C:H1L3000 2.2 56.3 1.0
C11 C:H1L3000 2.3 56.9 1.0
C13 C:H1L3000 2.7 60.7 1.0
C10 C:H1L3000 3.6 58.5 1.0
CB B:ALA1929 3.7 26.0 1.0
CG1 B:VAL1967 3.9 43.3 1.0
CA B:GLY1971 3.9 34.9 1.0
O B:VAL1967 4.0 40.0 1.0
CD1 B:ILE1974 4.0 17.2 1.0
C14 C:H1L3000 4.1 61.9 1.0
CG B:TRP1924 4.3 47.7 1.0
CD2 B:TRP1924 4.4 46.1 1.0
N B:GLY1971 4.6 35.6 1.0
CD1 B:TRP1924 4.6 48.2 1.0
CG1 B:VAL2002 4.7 22.6 1.0
CE2 B:TRP1924 4.7 46.3 1.0
N9 C:H1L3000 4.7 59.5 1.0
CB B:TRP1924 4.7 46.3 1.0
CA B:ALA1929 4.7 25.7 1.0
CE3 B:TRP1924 4.7 46.3 1.0
NE1 B:TRP1924 4.8 46.2 1.0
C9 C:H1L3000 4.9 60.3 1.0
C B:VAL1967 4.9 40.8 1.0

Fluorine binding site 9 out of 9 in 1uys

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Fluorine binding site 9 out of 9 in the Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 9 of Acetyl-Coa Carboxylase Carboxyltransferase Domain in Complex with Inhibitor Haloxyfop within 5.0Å range:
probe atom residue distance (Å) B Occ
C:F3000

b:54.0
occ:1.00
 F3 C:H1L3000 0.0 54.0 1.0
C12 C:H1L3000 1.3 55.3 1.0
F2 C:H1L3000 2.2 52.8 1.0
F1 C:H1L3000 2.2 56.3 1.0
C11 C:H1L3000 2.3 56.9 1.0
C10 C:H1L3000 3.0 58.5 1.0
CB B:TRP1924 3.1 46.3 1.0
CG B:TRP1924 3.2 47.7 1.0
CD2 B:TRP1924 3.2 46.1 1.0
CE3 B:TRP1924 3.3 46.3 1.0
C13 C:H1L3000 3.3 60.7 1.0
CB B:PHE1956 3.8 54.0 1.0
CG1 B:VAL1967 4.0 43.3 1.0
CD1 B:PHE1956 4.0 48.8 1.0
CD1 B:TRP1924 4.0 48.2 1.0
CE2 B:TRP1924 4.1 46.3 1.0
CG B:PHE1956 4.1 50.4 1.0
CZ3 B:TRP1924 4.2 49.3 1.0
N9 C:H1L3000 4.2 59.5 1.0
C14 C:H1L3000 4.5 61.9 1.0
NE1 B:TRP1924 4.5 46.2 1.0
CA B:TRP1924 4.6 45.5 1.0
C9 C:H1L3000 4.9 60.3 1.0
CZ2 B:TRP1924 4.9 46.6 1.0
CH2 B:TRP1924 4.9 47.4 1.0
CB B:ALA1929 4.9 26.0 1.0
CE1 B:PHE1956 5.0 48.4 1.0

Reference:

H.Zhang, B.Tweel, L.Tong. Molecular Basis For the Inhibition of the Carboxyltransferase Domain of Acetyl-Coenzyme-A Carboxylase By Haloxyfop and Diclofop Proc.Natl.Acad.Sci.Usa V. 101 5910 2004.
ISSN: ISSN 0027-8424
PubMed: 15079078
DOI: 10.1073/PNAS.0400891101
Page generated: Wed Jul 31 13:07:03 2024

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