Fluorine in PDB 8p42: Full Length Structure of Tcmip with Bound Inhibitor NJS227.

Enzymatic activity of Full Length Structure of Tcmip with Bound Inhibitor NJS227.

All present enzymatic activity of Full Length Structure of Tcmip with Bound Inhibitor NJS227.:
5.2.1.8;

Protein crystallography data

The structure of Full Length Structure of Tcmip with Bound Inhibitor NJS227., PDB code: 8p42 was solved by J.J.Whittaker, A.Guskov, B.Goretzki, U.A.Hellmich, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.88 / 2.64
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 87.744, 87.744, 57.505, 90, 90, 90
R / Rfree (%) 22.4 / 28.2

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Full Length Structure of Tcmip with Bound Inhibitor NJS227. (pdb code 8p42). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the Full Length Structure of Tcmip with Bound Inhibitor NJS227., PDB code: 8p42:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;

Fluorine binding site 1 out of 6 in 8p42

Go back to Fluorine Binding Sites List in 8p42
Fluorine binding site 1 out of 6 in the Full Length Structure of Tcmip with Bound Inhibitor NJS227.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Full Length Structure of Tcmip with Bound Inhibitor NJS227. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F201

b:51.0
occ:0.50
 F1 A:WRX201 0.0 51.0 0.5
F1 A:WRX201 0.1 51.0 0.5
C1 A:WRX201 1.4 47.9 0.5
C1 A:WRX201 1.4 47.9 0.5
C28 A:WRX201 2.3 48.4 0.5
C28 A:WRX201 2.3 48.4 0.5
C2 A:WRX201 2.3 42.2 0.5
C2 A:WRX201 2.4 42.2 0.5
C27 A:WRX201 3.6 43.3 0.5
C27 A:WRX201 3.6 43.3 0.5
C3 A:WRX201 3.6 41.9 0.5
O A:PHE73 3.6 52.2 1.0
CB A:PHE73 3.6 41.2 1.0
C3 A:WRX201 3.6 41.9 0.5
CB A:MET125 3.8 51.7 1.0
C4 A:WRX201 4.1 42.9 0.5
C4 A:WRX201 4.1 42.9 0.5
CD1 A:PHE73 4.2 42.3 1.0
CG A:MET125 4.2 58.9 1.0
N A:MET125 4.3 50.8 1.0
C A:PHE73 4.3 48.9 1.0
CG A:PHE73 4.3 43.9 1.0
CA A:PHE73 4.4 43.1 1.0
CA A:MET125 4.5 48.9 1.0
CG1 A:ILE126 4.6 42.8 1.0
O A:GLY122 4.6 50.3 1.0
C A:MET125 4.8 53.3 1.0
CD1 A:ILE126 5.0 37.7 1.0

Fluorine binding site 2 out of 6 in 8p42

Go back to Fluorine Binding Sites List in 8p42
Fluorine binding site 2 out of 6 in the Full Length Structure of Tcmip with Bound Inhibitor NJS227.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Full Length Structure of Tcmip with Bound Inhibitor NJS227. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F201

b:51.0
occ:0.50
 F1 A:WRX201 0.0 51.0 0.5
F1 A:WRX201 0.1 51.0 0.5
C1 A:WRX201 1.4 47.9 0.5
C1 A:WRX201 1.4 47.9 0.5
C2 A:WRX201 2.3 42.2 0.5
C28 A:WRX201 2.3 48.4 0.5
C2 A:WRX201 2.3 42.2 0.5
C28 A:WRX201 2.4 48.4 0.5
C3 A:WRX201 3.6 41.9 0.5
C27 A:WRX201 3.6 43.3 0.5
C3 A:WRX201 3.6 41.9 0.5
C27 A:WRX201 3.6 43.3 0.5
CB A:PHE73 3.6 41.2 1.0
O A:PHE73 3.7 52.2 1.0
CB A:MET125 3.8 51.7 1.0
C4 A:WRX201 4.1 42.9 0.5
C4 A:WRX201 4.1 42.9 0.5
N A:MET125 4.2 50.8 1.0
CG A:MET125 4.2 58.9 1.0
CD1 A:PHE73 4.2 42.3 1.0
CG A:PHE73 4.3 43.9 1.0
C A:PHE73 4.3 48.9 1.0
CA A:MET125 4.5 48.9 1.0
CA A:PHE73 4.5 43.1 1.0
CG1 A:ILE126 4.5 42.8 1.0
O A:GLY122 4.5 50.3 1.0
C A:MET125 4.7 53.3 1.0
CD1 A:ILE126 4.9 37.7 1.0
N A:GLY124 5.0 55.1 1.0

Fluorine binding site 3 out of 6 in 8p42

Go back to Fluorine Binding Sites List in 8p42
Fluorine binding site 3 out of 6 in the Full Length Structure of Tcmip with Bound Inhibitor NJS227.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Full Length Structure of Tcmip with Bound Inhibitor NJS227. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F201

b:49.2
occ:0.50
 F2 A:WRX201 0.0 49.2 0.5
F2 A:WRX201 0.1 49.2 0.5
C13 A:WRX201 1.3 42.3 0.5
C13 A:WRX201 1.4 42.3 0.5
C14 A:WRX201 2.2 39.0 0.5
C12 A:WRX201 2.3 40.4 0.5
C14 A:WRX201 2.3 39.0 0.5
C12 A:WRX201 2.3 40.4 0.5
O A:HOH334 3.1 43.6 1.0
C15 A:WRX201 3.5 38.9 0.5
C11 A:WRX201 3.5 41.0 0.5
C15 A:WRX201 3.6 38.9 0.5
C11 A:WRX201 3.6 41.0 0.5
C10 A:WRX201 4.0 38.2 0.5
C10 A:WRX201 4.1 38.2 0.5
O1 A:PEG202 4.5 45.4 1.0
C1 A:PEG202 4.5 48.1 1.0

Fluorine binding site 4 out of 6 in 8p42

Go back to Fluorine Binding Sites List in 8p42
Fluorine binding site 4 out of 6 in the Full Length Structure of Tcmip with Bound Inhibitor NJS227.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Full Length Structure of Tcmip with Bound Inhibitor NJS227. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F201

b:49.2
occ:0.50
 F2 A:WRX201 0.0 49.2 0.5
F2 A:WRX201 0.1 49.2 0.5
C13 A:WRX201 1.4 42.3 0.5
C13 A:WRX201 1.5 42.3 0.5
C14 A:WRX201 2.3 39.0 0.5
C12 A:WRX201 2.3 40.4 0.5
C12 A:WRX201 2.4 40.4 0.5
C14 A:WRX201 2.4 39.0 0.5
O A:HOH334 3.1 43.6 1.0
C15 A:WRX201 3.6 38.9 0.5
C11 A:WRX201 3.6 41.0 0.5
C11 A:WRX201 3.7 41.0 0.5
C15 A:WRX201 3.7 38.9 0.5
C10 A:WRX201 4.1 38.2 0.5
C10 A:WRX201 4.2 38.2 0.5
O1 A:PEG202 4.4 45.4 1.0
C1 A:PEG202 4.5 48.1 1.0

Fluorine binding site 5 out of 6 in 8p42

Go back to Fluorine Binding Sites List in 8p42
Fluorine binding site 5 out of 6 in the Full Length Structure of Tcmip with Bound Inhibitor NJS227.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Full Length Structure of Tcmip with Bound Inhibitor NJS227. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:F201

b:34.6
occ:1.00
 F1 D:WRX201 0.0 34.6 1.0
C1 D:WRX201 1.4 35.6 1.0
C2 D:WRX201 2.3 36.7 1.0
C28 D:WRX201 2.3 29.9 1.0
O D:HOH314 3.4 35.1 1.0
C27 D:WRX201 3.6 30.3 1.0
C3 D:WRX201 3.6 34.8 1.0
N D:GLY124 3.7 45.4 1.0
CA D:GLY123 3.9 44.3 1.0
CG D:MET125 3.9 39.0 1.0
O D:PHE73 4.0 24.8 1.0
C4 D:WRX201 4.1 30.8 1.0
N D:MET125 4.1 38.2 1.0
CB D:PHE73 4.1 25.0 1.0
N D:GLY123 4.2 40.1 1.0
C D:GLY123 4.3 46.1 1.0
CD1 D:PHE73 4.6 25.8 1.0
CG1 D:ILE126 4.7 31.6 1.0
C D:PHE73 4.7 24.4 1.0
CG D:PHE73 4.7 26.8 1.0
CA D:GLY124 4.8 39.7 1.0
N D:ILE126 4.8 36.3 1.0
C3 D:PEG202 4.8 40.2 1.0
CD1 D:ILE126 4.9 27.6 1.0
CA D:MET125 4.9 42.7 1.0
C D:GLY124 4.9 44.6 1.0
CA D:PHE73 4.9 24.8 1.0
C D:MET125 5.0 41.1 1.0

Fluorine binding site 6 out of 6 in 8p42

Go back to Fluorine Binding Sites List in 8p42
Fluorine binding site 6 out of 6 in the Full Length Structure of Tcmip with Bound Inhibitor NJS227.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Full Length Structure of Tcmip with Bound Inhibitor NJS227. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:F201

b:47.1
occ:1.00
 F2 D:WRX201 0.0 47.1 1.0
C13 D:WRX201 1.4 32.3 1.0
C14 D:WRX201 2.3 31.7 1.0
C12 D:WRX201 2.3 32.7 1.0
O2 D:PEG202 2.9 39.6 1.0
C15 D:WRX201 3.6 27.8 1.0
C11 D:WRX201 3.6 29.6 1.0
C3 D:PEG202 3.7 40.2 1.0
C2 D:PEG202 4.1 34.2 1.0
C10 D:WRX201 4.1 31.1 1.0
C4 D:PEG202 4.3 41.3 1.0
C1 D:PEG202 4.4 32.1 1.0

Reference:

J.J.Whittaker, A.Guskov, B.Goretzki, U.A.Hellmich. Structural Dynamics of Macrophage Infectivity Potentiator Proteins (Mips) Are Differentially Modulated By Inhibitors and Appendage Domains To Be Published.
Page generated: Fri Aug 2 21:43:30 2024

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