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Fluorine in PDB 4g2r: Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis

Enzymatic activity of Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis

All present enzymatic activity of Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis:
6.4.1.3;

Protein crystallography data

The structure of Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis, PDB code: 4g2r was solved by M.C.M.Reddy, J.B.Bruning, C.Thurman, M.Sherekar, S.Valluru, H.Ehrenfeld, J.C.Sacchettini, Tb Structural Genomics Consortium (Tbsgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 58.94 / 2.28
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 117.780, 126.240, 161.700, 90.00, 90.00, 90.00
R / Rfree (%) 16.4 / 19.8

Other elements in 4g2r:

The structure of Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis also contains other interesting chemical elements:

Chlorine (Cl) 4 atoms

Fluorine Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Fluorine atom in the Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis (pdb code 4g2r). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 12 binding sites of Fluorine where determined in the Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis, PDB code: 4g2r:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Fluorine binding site 1 out of 12 in 4g2r

Go back to Fluorine Binding Sites List in 4g2r
Fluorine binding site 1 out of 12 in the Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis


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 the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F501

b:41.6
occ:1.00
 F1 A:H1L501 0.0 41.6 1.0
C12 A:H1L501 1.3 44.0 1.0
F3 A:H1L501 2.2 47.7 1.0
F2 A:H1L501 2.2 42.4 1.0
C11 A:H1L501 2.3 48.2 1.0
C13 A:H1L501 2.7 47.1 1.0
CG2 B:VAL337 3.5 32.9 1.0
C10 A:H1L501 3.6 38.6 1.0
O B:VAL337 3.6 29.8 1.0
CA B:GLY341 3.7 30.4 1.0
C14 A:H1L501 4.1 53.2 1.0
CB B:TYR326 4.2 33.7 1.0
OH A:TYR141 4.3 70.8 1.0
N B:GLY341 4.4 24.6 1.0
CB B:LEU295 4.4 27.9 1.0
C B:VAL337 4.5 31.9 1.0
CG B:TYR326 4.5 40.5 1.0
N9 A:H1L501 4.7 40.8 1.0
CD1 B:LEU295 4.7 20.4 1.0
CB B:ALA300 4.7 17.7 1.0
CB B:VAL337 4.8 31.7 1.0
CD2 B:TYR326 4.8 41.7 1.0
C B:GLY341 4.9 31.3 1.0
C9 A:H1L501 4.9 47.6 1.0

Fluorine binding site 2 out of 12 in 4g2r

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Fluorine binding site 2 out of 12 in the Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F501

b:42.4
occ:1.00
 F2 A:H1L501 0.0 42.4 1.0
C12 A:H1L501 1.3 44.0 1.0
F3 A:H1L501 2.2 47.7 1.0
F1 A:H1L501 2.2 41.6 1.0
C11 A:H1L501 2.3 48.2 1.0
C10 A:H1L501 2.8 38.6 1.0
CB B:ALA370 3.3 21.8 1.0
C13 A:H1L501 3.5 47.1 1.0
CA B:GLY341 3.8 30.4 1.0
CD1 B:LEU295 4.1 20.4 1.0
N9 A:H1L501 4.1 40.8 1.0
OH A:TYR141 4.3 70.8 1.0
O B:GLY341 4.3 36.9 1.0
C B:GLY341 4.4 31.3 1.0
C14 A:H1L501 4.6 53.2 1.0
O B:GLY366 4.8 28.3 1.0
CA B:ALA370 4.8 25.6 1.0
C9 A:H1L501 4.8 47.6 1.0
CD2 B:LEU344 4.9 26.6 1.0
CZ A:TYR141 4.9 60.2 1.0
CA B:ALA367 5.0 25.9 1.0

Fluorine binding site 3 out of 12 in 4g2r

Go back to Fluorine Binding Sites List in 4g2r
Fluorine binding site 3 out of 12 in the Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F501

b:47.7
occ:1.00
 F3 A:H1L501 0.0 47.7 1.0
C12 A:H1L501 1.3 44.0 1.0
F1 A:H1L501 2.2 41.6 1.0
F2 A:H1L501 2.2 42.4 1.0
C11 A:H1L501 2.3 48.2 1.0
C10 A:H1L501 3.0 38.6 1.0
CD1 B:LEU295 3.3 20.4 1.0
C13 A:H1L501 3.3 47.1 1.0
CB B:LEU295 3.5 27.9 1.0
CB B:TYR326 3.6 33.7 1.0
CD2 B:TYR326 3.7 41.7 1.0
CG B:TYR326 3.9 40.5 1.0
CA B:ALA367 3.9 25.9 1.0
CG B:LEU295 4.0 30.0 1.0
N9 A:H1L501 4.2 40.8 1.0
CB B:ALA367 4.2 30.2 1.0
N B:ALA367 4.4 25.5 1.0
CB B:ALA370 4.5 21.8 1.0
C14 A:H1L501 4.5 53.2 1.0
CE2 B:TYR326 4.7 47.7 1.0
CA B:TYR326 4.8 33.3 1.0
C9 A:H1L501 4.8 47.6 1.0
C B:GLY366 4.8 32.6 1.0
CA B:LEU295 4.9 31.3 1.0
O B:GLY366 4.9 28.3 1.0
CG2 B:VAL337 4.9 32.9 1.0
CD1 B:TYR326 5.0 46.0 1.0

Fluorine binding site 4 out of 12 in 4g2r

Go back to Fluorine Binding Sites List in 4g2r
Fluorine binding site 4 out of 12 in the Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F502

b:55.6
occ:1.00
 F1 A:H1L502 0.0 55.6 1.0
C12 A:H1L502 1.3 62.5 1.0
F3 A:H1L502 2.2 75.8 1.0
F2 A:H1L502 2.2 66.0 1.0
C11 A:H1L502 2.3 51.5 1.0
C13 A:H1L502 3.1 38.7 1.0
C10 A:H1L502 3.3 49.9 1.0
CG2 A:VAL131 3.6 37.3 1.0
CG2 A:VAL157 3.6 47.0 1.0
CB A:PRO143 4.2 28.9 1.0
O A:ALA140 4.2 43.7 1.0
SD A:MET151 4.3 50.1 1.0
C14 A:H1L502 4.3 41.4 1.0
CG1 A:VAL131 4.4 38.7 1.0
CG1 A:VAL149 4.4 27.6 1.0
CE A:MET151 4.4 47.9 1.0
CG A:PRO143 4.4 29.2 1.0
N9 A:H1L502 4.4 52.8 1.0
CB A:VAL131 4.5 37.1 1.0
CG A:MET151 4.6 36.1 1.0
C9 A:H1L502 4.9 52.0 1.0
CB A:VAL157 4.9 49.4 1.0
CA A:ALA140 4.9 47.8 1.0

Fluorine binding site 5 out of 12 in 4g2r

Go back to Fluorine Binding Sites List in 4g2r
Fluorine binding site 5 out of 12 in the Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F502

b:66.0
occ:1.00
 F2 A:H1L502 0.0 66.0 1.0
C12 A:H1L502 1.3 62.5 1.0
F1 A:H1L502 2.2 55.6 1.0
F3 A:H1L502 2.2 75.8 1.0
C11 A:H1L502 2.3 51.5 1.0
C13 A:H1L502 2.7 38.7 1.0
CB A:PRO143 3.1 28.9 1.0
C10 A:H1L502 3.5 49.9 1.0
O A:ALA140 3.7 43.7 1.0
CG1 A:VAL149 3.8 27.6 1.0
CG1 A:VAL190 3.8 45.0 1.0
N A:ALA144 3.9 28.4 1.0
CG A:PRO143 4.0 29.2 1.0
C14 A:H1L502 4.0 41.4 1.0
CG2 A:VAL149 4.1 30.2 1.0
C A:PRO143 4.1 25.2 1.0
CA A:PRO143 4.2 28.9 1.0
CB A:VAL149 4.5 33.1 1.0
CA A:ALA144 4.5 27.4 1.0
N9 A:H1L502 4.6 52.8 1.0
CG2 A:VAL131 4.7 37.3 1.0
O A:VAL190 4.7 46.6 1.0
CD A:PRO143 4.8 23.2 1.0
C9 A:H1L502 4.8 52.0 1.0
O A:PRO143 4.8 37.5 1.0
C A:ALA140 4.8 49.7 1.0
N A:PRO143 4.9 28.2 1.0
CB A:ALA144 4.9 34.0 1.0
CB A:VAL190 4.9 50.0 1.0

Fluorine binding site 6 out of 12 in 4g2r

Go back to Fluorine Binding Sites List in 4g2r
Fluorine binding site 6 out of 12 in the Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F502

b:75.8
occ:1.00
 F3 A:H1L502 0.0 75.8 1.0
C12 A:H1L502 1.3 62.5 1.0
F1 A:H1L502 2.2 55.6 1.0
F2 A:H1L502 2.2 66.0 1.0
C11 A:H1L502 2.3 51.5 1.0
C10 A:H1L502 2.8 49.9 1.0
CG1 A:VAL149 3.4 27.6 1.0
SD A:MET151 3.4 50.1 1.0
C13 A:H1L502 3.6 38.7 1.0
CG A:MET151 4.0 36.1 1.0
N9 A:H1L502 4.1 52.8 1.0
CA A:CYS191 4.2 35.5 1.0
N A:CYS191 4.2 32.5 1.0
CB A:CYS191 4.2 32.7 1.0
CG1 A:VAL190 4.2 45.0 1.0
O A:VAL190 4.3 46.6 1.0
C A:VAL190 4.3 38.9 1.0
CB A:VAL149 4.3 33.1 1.0
CE A:MET151 4.4 47.9 1.0
CB A:VAL190 4.6 50.0 1.0
CG2 A:VAL131 4.6 37.3 1.0
CG2 A:VAL149 4.6 30.2 1.0
C14 A:H1L502 4.7 41.4 1.0
CG2 A:VAL157 4.8 47.0 1.0
C9 A:H1L502 4.9 52.0 1.0
CB A:PRO143 4.9 28.9 1.0

Fluorine binding site 7 out of 12 in 4g2r

Go back to Fluorine Binding Sites List in 4g2r
Fluorine binding site 7 out of 12 in the Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 7 of Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F501

b:53.8
occ:1.00
 F1 B:H1L501 0.0 53.8 1.0
C12 B:H1L501 1.3 46.0 1.0
F3 B:H1L501 2.2 46.2 1.0
F2 B:H1L501 2.2 45.5 1.0
C11 B:H1L501 2.3 47.1 1.0
C13 B:H1L501 2.6 51.6 1.0
CA A:GLY341 3.4 27.4 1.0
O A:VAL337 3.4 31.3 1.0
CG2 A:VAL337 3.5 38.3 1.0
C10 B:H1L501 3.6 40.7 1.0
C14 B:H1L501 4.0 58.4 1.0
OH B:TYR141 4.2 63.5 1.0
N A:GLY341 4.2 28.0 1.0
CB A:TYR326 4.4 36.1 1.0
C A:VAL337 4.4 32.5 1.0
C A:GLY341 4.6 33.9 1.0
N9 B:H1L501 4.7 44.3 1.0
CB A:LEU295 4.7 27.6 1.0
CG A:TYR326 4.7 36.1 1.0
CB A:ALA300 4.7 21.1 1.0
CB A:VAL337 4.8 37.0 1.0
CD1 A:LEU295 4.8 30.6 1.0
C9 B:H1L501 4.9 50.3 1.0
CZ B:TYR141 4.9 57.5 1.0
CD2 A:TYR326 4.9 39.0 1.0
CA A:VAL337 4.9 39.0 1.0
O A:GLY341 4.9 31.0 1.0

Fluorine binding site 8 out of 12 in 4g2r

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Fluorine binding site 8 out of 12 in the Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 8 of Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F501

b:45.5
occ:1.00
 F2 B:H1L501 0.0 45.5 1.0
C12 B:H1L501 1.3 46.0 1.0
F3 B:H1L501 2.2 46.2 1.0
F1 B:H1L501 2.2 53.8 1.0
C11 B:H1L501 2.3 47.1 1.0
C10 B:H1L501 2.8 40.7 1.0
CB A:ALA370 3.5 24.8 1.0
C13 B:H1L501 3.5 51.6 1.0
CA A:GLY341 3.7 27.4 1.0
CD1 A:LEU295 4.1 30.6 1.0
O A:GLY341 4.1 31.0 1.0
N9 B:H1L501 4.1 44.3 1.0
C A:GLY341 4.3 33.9 1.0
OH B:TYR141 4.3 63.5 1.0
C14 B:H1L501 4.7 58.4 1.0
O A:GLY366 4.7 27.9 1.0
CD2 A:LEU344 4.8 20.0 1.0
C9 B:H1L501 4.9 50.3 1.0
CZ B:TYR141 4.9 57.5 1.0
N A:GLY341 4.9 28.0 1.0
CA A:ALA370 5.0 29.0 1.0

Fluorine binding site 9 out of 12 in 4g2r

Go back to Fluorine Binding Sites List in 4g2r
Fluorine binding site 9 out of 12 in the Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 9 of Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F501

b:46.2
occ:1.00
 F3 B:H1L501 0.0 46.2 1.0
C12 B:H1L501 1.3 46.0 1.0
F1 B:H1L501 2.2 53.8 1.0
F2 B:H1L501 2.2 45.5 1.0
C11 B:H1L501 2.3 47.1 1.0
C10 B:H1L501 3.1 40.7 1.0
C13 B:H1L501 3.3 51.6 1.0
CD1 A:LEU295 3.3 30.6 1.0
CB A:LEU295 3.5 27.6 1.0
CB A:TYR326 3.5 36.1 1.0
CD2 A:TYR326 3.8 39.0 1.0
CG A:TYR326 4.0 36.1 1.0
CG A:LEU295 4.0 34.8 1.0
CA A:ALA367 4.2 28.8 1.0
N9 B:H1L501 4.3 44.3 1.0
C14 B:H1L501 4.5 58.4 1.0
CB A:ALA367 4.5 27.8 1.0
N A:ALA367 4.6 26.1 1.0
CG2 A:VAL337 4.7 38.3 1.0
CB A:ALA370 4.7 24.8 1.0
CA A:TYR326 4.8 38.8 1.0
CE2 A:TYR326 4.8 43.5 1.0
C9 B:H1L501 4.8 50.3 1.0
CA A:LEU295 4.9 28.6 1.0
CD2 A:LEU295 5.0 32.2 1.0

Fluorine binding site 10 out of 12 in 4g2r

Go back to Fluorine Binding Sites List in 4g2r
Fluorine binding site 10 out of 12 in the Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 10 of Crystal Structure of the Carboxyltransferase Subunit of Acc (ACCD6) in Complex with Inhibitor Haloxyfop From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F502

b:54.1
occ:1.00
 F1 B:H1L502 0.0 54.1 1.0
C12 B:H1L502 1.3 55.4 1.0
F3 B:H1L502 2.2 66.4 1.0
F2 B:H1L502 2.2 55.8 1.0
C11 B:H1L502 2.3 49.3 1.0
C13 B:H1L502 3.0 39.7 1.0
C10 B:H1L502 3.3 51.8 1.0
CG2 B:VAL157 3.5 44.3 1.0
CG2 B:VAL131 3.6 30.5 1.0
O B:ALA140 3.9 43.5 1.0
C14 B:H1L502 4.2 49.5 1.0
CG1 B:VAL131 4.4 37.4 1.0
CB B:PRO143 4.4 32.2 1.0
CB B:VAL131 4.4 38.3 1.0
CA B:ALA140 4.5 49.0 1.0
N9 B:H1L502 4.5 49.9 1.0
CG B:PRO143 4.6 39.2 1.0
SD B:MET151 4.6 53.5 1.0
C B:ALA140 4.6 45.9 1.0
CG1 B:VAL149 4.7 32.5 1.0
CB B:VAL157 4.8 48.0 1.0
CE B:MET151 4.8 38.8 1.0
CB B:ALA140 4.8 49.4 1.0
CB B:ALA135 4.8 36.4 1.0
CG1 B:VAL157 4.8 50.3 1.0
C9 B:H1L502 4.8 51.1 1.0
CG B:MET151 4.9 36.6 1.0

Reference:

M.C.Reddy, A.Breda, J.B.Bruning, M.Sherekar, S.Valluru, C.Thurman, H.Ehrenfeld, J.C.Sacchettini. Structure, Activity, and Inhibition of the Carboxyltransferase Beta-Subunit of Acetyl Coenzyme A Carboxylase (ACCD6) From Mycobacterium Tuberculosis. Antimicrob.Agents Chemother. V. 58 6122 2014.
ISSN: ISSN 0066-4804
PubMed: 25092705
DOI: 10.1128/AAC.02574-13
Page generated: Thu Aug 1 01:44:40 2024

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