Fluorine in PDB 8p3d: Full Length Structure of Tcmip with Bound Inhibitor NJS224.

Enzymatic activity of Full Length Structure of Tcmip with Bound Inhibitor NJS224.

All present enzymatic activity of Full Length Structure of Tcmip with Bound Inhibitor NJS224.:
5.2.1.8;

Protein crystallography data

The structure of Full Length Structure of Tcmip with Bound Inhibitor NJS224., PDB code: 8p3d 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) 46.77 / 1.71
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 46.858, 34.696, 53.081, 90, 93.53, 90
R / Rfree (%) 18.2 / 21.7

Other elements in 8p3d:

The structure of Full Length Structure of Tcmip with Bound Inhibitor NJS224. also contains other interesting chemical elements:

Sodium (Na) 4 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Full Length Structure of Tcmip with Bound Inhibitor NJS224. (pdb code 8p3d). 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 Full Length Structure of Tcmip with Bound Inhibitor NJS224., PDB code: 8p3d:

Fluorine binding site 1 out of 1 in 8p3d

Go back to Fluorine Binding Sites List in 8p3d
Fluorine binding site 1 out of 1 in the Full Length Structure of Tcmip with Bound Inhibitor NJS224.


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 NJS224. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F201

b:26.5
occ:1.00
F1 A:WS5201 0.0 26.5 1.0
C1 A:WS5201 1.4 22.5 1.0
C2 A:WS5201 2.3 21.6 1.0
C25 A:WS5201 2.3 26.6 1.0
HB2 A:MET125 2.5 27.6 1.0
H1 A:WS5201 2.5 25.9 1.0
H33 A:WS5201 2.5 31.9 1.0
HA3 A:GLY123 2.7 31.6 1.0
HB2 A:PHE73 3.0 25.3 1.0
H A:MET125 3.2 29.4 1.0
HG13 A:ILE126 3.3 24.7 1.0
CB A:MET125 3.4 23.0 1.0
C3 A:WS5201 3.6 21.5 1.0
C24 A:WS5201 3.6 23.6 1.0
CA A:GLY123 3.6 26.3 1.0
O A:GLY123 3.6 27.7 1.0
HG3 A:MET125 3.7 36.5 1.0
O A:GLY122 3.8 22.8 1.0
C A:GLY123 3.8 28.1 1.0
CB A:PHE73 3.9 21.1 1.0
HD1 A:PHE73 3.9 23.6 1.0
CG A:MET125 4.0 30.4 1.0
HB3 A:MET125 4.0 27.6 1.0
N A:MET125 4.0 24.5 1.0
H A:ILE126 4.0 25.1 1.0
C4 A:WS5201 4.1 21.0 1.0
HD11 A:ILE126 4.1 24.7 1.0
HA2 A:GLY123 4.2 31.6 1.0
CG1 A:ILE126 4.2 20.6 1.0
CA A:MET125 4.2 25.1 1.0
HB3 A:PHE73 4.2 25.3 1.0
SD A:MET125 4.3 29.4 1.0
O A:PHE73 4.3 22.6 1.0
H2 A:WS5201 4.3 25.8 1.0
H32 A:WS5201 4.4 28.4 1.0
N A:ILE126 4.4 20.9 1.0
N A:GLY123 4.5 27.2 1.0
C A:GLY122 4.5 26.4 1.0
CD1 A:PHE73 4.5 19.7 1.0
HD12 A:ILE126 4.5 24.7 1.0
CD1 A:ILE126 4.5 20.6 1.0
CG A:PHE73 4.5 17.7 1.0
C A:MET125 4.6 23.5 1.0
HG12 A:ILE126 4.7 24.7 1.0
N A:GLY124 4.7 28.9 1.0
O A:HOH453 4.9 46.3 1.0
HG2 A:MET125 4.9 36.5 1.0
C A:PHE73 4.9 20.5 1.0
CA A:PHE73 4.9 15.8 1.0
HA A:PHE73 4.9 19.0 1.0
HB A:ILE126 4.9 23.6 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 21:42:29 2024

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